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Mix Mistress Alice💄"The most dangerous aspect of this trade-off isn’t the loss of privacy—it’s the loss of awareness that we’re losing anything at all. We’re not just losing skills and privacy; we’re losing the ability to recognize what independence feels like. The question isn’t whether convenience is worth the cost of liberty—it’s whether we’ll recognize what we’ve lost before we forget we ever had it."—Josh Stylman ><a href="https://truthunmuted.org/digital-control-how-engineered-dependency-erases-our-autonomy/" rel="nofollow noopener noreferrer" translate="no" target="_blank">https://truthunmuted.org/digital-control-how-engineered-dependency-erases-our-autonomy/</a><a href="https://todon.eu/tags/dependency" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#dependency</a> <a href="https://todon.eu/tags/convenience" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#convenience</a> <a href="https://todon.eu/tags/surveillance" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#surveillance</a> <a href="https://todon.eu/tags/amnesia" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#amnesia</a> <a href="https://todon.eu/tags/security" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#security</a> <a href="https://todon.eu/tags/socialmedia" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#socialmedia</a> <a href="https://todon.eu/tags/smartfeatures" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#smartfeatures</a> <a href="https://todon.eu/tags/disconnection" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#disconnection</a> <a href="https://todon.eu/tags/appintegration" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#appintegration</a> <a href="https://todon.eu/tags/CBDC" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#CBDC</a> <a href="https://todon.eu/tags/compliance" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#compliance</a> <a href="https://todon.eu/tags/AI" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#AI</a> <a href="https://todon.eu/tags/atrophy" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#atrophy</a> <a href="https://todon.eu/tags/dumbingdown" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#dumbingdown</a> vs <a href="https://todon.eu/tags/autonomy" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#autonomy</a> <a href="https://todon.eu/tags/awareness" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#awareness</a> <a href="https://todon.eu/tags/craftsmanship" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#craftsmanship</a> <a href="https://todon.eu/tags/problemssolving" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#problemssolving</a> <a href="https://todon.eu/tags/community" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#community</a> <a href="https://todon.eu/tags/skills" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#skills</a> <a href="https://todon.eu/tags/makers" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#makers</a> <a href="https://todon.eu/tags/writing" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#writing</a> <a href="https://todon.eu/tags/literacy" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#literacy</a> <a href="https://todon.eu/tags/health" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#health</a> <a href="https://todon.eu/tags/wellbeing" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#wellbeing</a> <a href="https://todon.eu/tags/independence" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#independence</a> <a href="https://todon.eu/tags/freedom" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#freedom</a> <a href="https://todon.eu/tags/capability" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#capability</a> <a href="https://todon.eu/tags/selfagency" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#selfagency</a> <a href="https://todon.eu/tags/DigitalControl" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#DigitalControl</a>

Joseph P.How Mitochondrial Dynamism Orchestrates MitophagyAuthors Orian S. Shirihai, Moshi Song, Gerald W. Dorn II<a href="https://qoto.org/tags/explainpaper" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#explainpaper</a> <a href="https://a.gup.pe/u/explainpaper" class="u-url mention" rel="nofollow noopener noreferrer" target="_blank">@explainpaper</a> Understanding the Significance of Mitochondrial Fission and FusionMitochondrial dynamics refers to the movement of <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a> within a cell. This includes <a href="https://qoto.org/tags/fission" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#fission</a>, which is when mitochondria divide into two parts, <a href="https://qoto.org/tags/fusion" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#fusion</a>, which is when two mitochondria join together, and <a href="https://qoto.org/tags/translocation" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#translocation</a>, which is when mitochondria move from one part of the <a href="https://qoto.org/tags/cell" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#cell</a> to another. This movement is important for maintaining the stability of the mitochondrial <a href="https://qoto.org/tags/DNA" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#DNA</a>, which is the genetic material found in mitochondria, and for controlling the cell's <a href="https://qoto.org/tags/respiration" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#respiration</a>. It can also be involved in programmed <a href="https://qoto.org/tags/CellDeath" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#CellDeath</a>. In the <a href="https://qoto.org/tags/heart" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#heart</a>, mitochondrial dynamics <a href="https://qoto.org/tags/protein" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#protein</a> s, such as <a href="https://qoto.org/tags/mitofusin" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitofusin</a> s, optic <a href="https://qoto.org/tags/atrophy" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#atrophy</a>, and dynamin-related protein, are highly expressed and play an important role in maintaining the quality of the <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a>. Other roles for mitochondrial dynamics proteins in the <a href="https://qoto.org/tags/heart" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#heart</a> include helping to move <a href="https://qoto.org/tags/calcium" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#calcium</a> into the mitochondria and regulating the structure of the mitochondria.<a href="https://qoto.org/tags/Mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#Mitochondria</a> are organelles in cells that are responsible for producing <a href="https://qoto.org/tags/energy" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#energy</a>. They can change their structure by breaking apart (<a href="https://qoto.org/tags/fission" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#fission</a>) and reforming (<a href="https://qoto.org/tags/fusion" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#fusion</a>). This process is complicated and energy intensive, so it is important to understand why it is necessary. One reason may be that when cells divide, the mitochondria need to be divided equally between the two daughter cells. This requires the <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a> to be broken apart and then reformed in each daughter <a href="https://qoto.org/tags/cell" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#cell</a>. This process of breaking apart and reforming is more efficient than growing and budding the mitochondria. To help explain this process, the authors use the analogy of an army. Each soldier in the army is like a protein in the mitochondria, and the different units of the army are like the different parts of the <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a>. To increase the size of the army, units are added, rather than individual soldiers. This is similar to how mitochondria are modified, by adding or subtracting intact functional units, rather than individual <a href="https://qoto.org/tags/protein" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#protein</a> s.Mitochondria are <a href="https://qoto.org/tags/organelle" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#organelle</a> s in cells that can change their physical structure by undergoing fission. Fission can be symmetrical, which is when mitochondria replicate and expand the number of <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a> in the <a href="https://qoto.org/tags/cell" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#cell</a>, or asymmetrical, which is when damaged components of the mitochondria are removed. The major <a href="https://qoto.org/tags/protein" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#protein</a> that helps with mitochondrial fission is called Drp1. It is mostly found in the <a href="https://qoto.org/tags/cytosol" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#cytosol</a>, but it needs to be recruited to the outer mitochondrial <a href="https://qoto.org/tags/membrane" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#membrane</a> to help with fission. Different factors can cause Drp1 to be recruited, such as phosphorylation by mitotic kinase cyclin B–cyclin-dependent-kinase (cdk) 1 complex during <a href="https://qoto.org/tags/cell" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#cell</a> division, or interacting with Bcl-2–associated protein x during <a href="https://qoto.org/tags/apoptosis" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#apoptosis</a>. Inhibiting Drp1 can protect cells from some, but not all, forms of programmed cell death.Mitochondria, which are organelles in cells, can be partitioned in <a href="https://qoto.org/tags/mitosis" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitosis</a>. The most efficient way to do this is by dismantling and then reconstituting the cellular <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a> network through sequential <a href="https://qoto.org/tags/organelle" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#organelle</a> fission, distribution, and refusion. To explain this concept, the text uses an analogy of how military units are constituted and managed within an army's hierarchical organization structure. In this analogy, each soldier represents an individual respiratory complex <a href="https://qoto.org/tags/protein" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#protein</a>, which are grouped together to form a squad (analogous to a respiratory complex). Squads are arranged into platoons, and approximately 6 platoons comprise a functional unit, the company (like 1 complete respiratory chain). The text suggests that it would be easier to add prefabricated supercomplexes to preexisting ones, as by fusing mitochondrial cristae, rather than trying to make a larger or different shaped mitochondrion through the wholesale incorporation of individual proteins. This is because making major structural modifications of respiratory supercomplexes on paracrystalline cristal membranes would first require destabilizing the <a href="https://qoto.org/tags/membrane" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#membrane</a>, then incorporating additional individual <a href="https://qoto.org/tags/protein" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#protein</a> components, and finally reconstructing the original highly organized structure, which is complicated and potentially disruptive.<a href="https://qoto.org/tags/Mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#Mitochondria</a> are small organelles in cells that can change their physical structure by undergoing fission. Fission can be symmetrical, which means the <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a> are split into two equal parts, or asymmetrical, which means the mitochondria are split into two unequal parts. Symmetrical fission is used to replicate and expand the number of mitochondria in the <a href="https://qoto.org/tags/cell" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#cell</a>, while asymmetrical fission is used to remove damaged mitochondria from the cell. The major <a href="https://qoto.org/tags/protein" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#protein</a> responsible for mitochondrial fission is called Drp1. Drp1 is mostly found in the cytosol, but it needs to be recruited to the outer mitochondrial <a href="https://qoto.org/tags/membrane" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#membrane</a> to promote fission. Different factors can stimulate Drp1 to move to the outer mitochondrial <a href="https://qoto.org/tags/membrane" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#membrane</a>, such as phosphorylation by mitotic kinase cyclin B–cyclin-dependent-kinase (cdk) 1 complex. In addition, the endoplasmic reticulum (ER) is often found at the sites of mitochondrial fission. If Drp1 is not present, the mitochondria can still fragment during <a href="https://qoto.org/tags/mitosis" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitosis</a>, suggesting that there are other mechanisms that can promote mitochondrial fission.The text is talking about the process of mitochondrial fission, which is a process that involves connecting and separating parts of a <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a>. The author uses the metaphor of making sausage links to explain the process, but then goes on to explain that mitochondria are actually more like a turducken, which is a dish made of a chicken stuffed inside a duck stuffed inside a turkey. This creates layers of poultry, which is similar to the double <a href="https://qoto.org/tags/membrane" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#membrane</a> /double space structure of <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a>. The author then explains that the process of mitochondrial fusion involves connecting the two mitochondria layer by layer, using proteins called mitofusins. Mitofusins have a <a href="https://qoto.org/tags/GTPase" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#GTPase</a> domain, two hydrophobic heptad repeat coiled-coil domains, and a small hydrophobic transmembrane domain. These proteins insert into the outer <a href="https://qoto.org/tags/membrane" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#membrane</a> of the <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a>, and can interact with other proteins in the cytosol. The process of mitochondrial fusion is GTP-independent and reversible, but <a href="https://qoto.org/tags/GTP" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#GTP</a> <a href="https://qoto.org/tags/hydrolysis" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#hydrolysis</a> is essential for irreversible outer membrane fusion.<a href="https://qoto.org/tags/Mitofusins" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#Mitofusins</a> are proteins that are essential for the first two stages of mitochondrial fusion, which is the process of two mitochondria joining together. This process is important for the exchange of information between the <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a> and the <a href="https://qoto.org/tags/cell" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#cell</a>. If the mitofusins are deleted or suppressed, the mitochondria become abnormally small and are unable to undergo normal fusion. This can have serious implications for the health of the <a href="https://qoto.org/tags/cell" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#cell</a>.Membrane-by-membrane mitochondrial fusion is a process that helps to keep the structure of the inner and outer membranes of <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a> intact. This helps to preserve the process of oxidative phosphorylation, which is important for providing energy to cells. Without this process, molecules that can be toxic to cells can form and interrupt the electron transport chain. This process is also important for maintaining the normal shape of the crista, which is necessary for the proper assembly and functioning of electron transport chain supercomplexes. In addition, it has been shown that interrupting Mfn-mediated OMM fusion can cause a <a href="https://qoto.org/tags/cardiomyocyte" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#cardiomyocyte</a> ER stress response, while interrupting Opa1-mediated IMM fusion can compromise mitochondrial function.Mitochondrial fission and fusion are important processes in <a href="https://qoto.org/tags/biology" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#biology</a>, as evidenced by the fact that mutations in genes related to these processes can cause serious diseases in humans. Altering the balance between fission and fusion can have an effect on the shape of <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a>, with more fusion leading to longer, more interconnected mitochondria, and more fission leading to shorter, less interconnected mitochondria. It is generally thought that more interconnected <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a> are healthier, but this is not always the case. In some cases, mitochondrial <a href="https://qoto.org/tags/fragmentation" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#fragmentation</a> can be beneficial, and it is important to understand the interplay between mitochondrial fragmentation and other processes, such as <a href="https://qoto.org/tags/mitophagy" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitophagy</a>, in order to understand the effects of mitochondrial fission and fusion.Mitophagy is a process by which cells eat their own <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a>. Mitochondria are organelles that produce energy in the form of <a href="https://qoto.org/tags/ATP" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#ATP</a>, which is used to power most biological processes. Over time, mitochondria can become damaged and produce toxic levels of reactive oxygen species ( <a href="https://qoto.org/tags/ROS" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#ROS</a> ). To protect the <a href="https://qoto.org/tags/cell" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#cell</a> from this damage, it has developed a sophisticated system to identify and remove these dysfunctional <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a>. This process is called mitophagy. <a href="https://qoto.org/tags/Mitophagy" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#Mitophagy</a> is a combination of the words mitochondria and <a href="https://qoto.org/tags/autophagy" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#autophagy</a>, which means "self-eating". It is a way for cells to selectively target and remove damaged mitochondria, while still keeping healthy ones. This helps to maintain the balance between having enough energy-producing <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a> and getting rid of the ones that are no longer functioning properly.Pulse chase experiments are a type of scientific experiment used to study the behavior of molecules over time. In this particular experiment, researchers found that when <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a> (the energy-producing organelles in cells) are targeted for <a href="https://qoto.org/tags/mitophagy" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitophagy</a> (a process of removing damaged mitochondria from the cell), they have a relatively depolarized <a href="https://qoto.org/tags/membrane" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#membrane</a> potential before being removed. This means that the <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a> have a lower electrical charge than normal, and they are less likely to be involved in <a href="https://qoto.org/tags/fusion" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#fusion</a> events (when two mitochondria join together). The time between the mitochondria becoming depolarized and being removed from the cell can range from less than an hour to about three hours, suggesting that there is a population of preautophagic <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a> (mitochondria that are about to be removed). This <a href="https://qoto.org/tags/preautophagic" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#preautophagic</a> pool helps to explain the variation in mitochondrial <a href="https://qoto.org/tags/membrane" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#membrane</a> potential in different cell types. The process that feeds mitochondria into the preautophagic pool is important for determining how quickly <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a> are removed from the <a href="https://qoto.org/tags/cell" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#cell</a>. Scientists have developed a technology to label individual mitochondria and track their <a href="https://qoto.org/tags/membrane" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#membrane</a> potential, which has allowed them to identify the event at which depolarized <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a> are produced. This event is called asymmetrical fission, and it occurs when the daughter mitochondria produced by the fission event have different <a href="https://qoto.org/tags/membrane" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#membrane</a> potentials - one daughter has a higher membrane potential than the mother mitochondrion, while the other daughter has a lower membrane potential. This process of asymmetrical fission helps to separate damaged components from healthy components before they are removed from the <a href="https://qoto.org/tags/cell" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#cell</a>.The concept of mitochondrial fission and fusion and how it affects mitochondrial quality. It suggests that when the fusion factors Mfn1 and Mfn2 are both absent, unusually small and degenerated <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a> accumulate in adult mouse hearts. This was associated with impaired <a href="https://qoto.org/tags/cardiomyocyte" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#cardiomyocyte</a> respiration, but not with measurable alterations in <a href="https://qoto.org/tags/oxygen" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#oxygen</a> consumption. It was later discovered that the isolation procedure used was not capturing the fragmented <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a> produced by interrupting mitochondrial fusion. This led to the discovery that Mfn2 is essential to <a href="https://qoto.org/tags/Parkin" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#Parkin</a>-mediated <a href="https://qoto.org/tags/mitophagy" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitophagy</a>, which is a process that helps to maintain mitochondrial quality. Three recent papers have also implicated the mitochondrial fission protein Drp1 in cardiac <a href="https://qoto.org/tags/mitophagy" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitophagy</a>, and it is suggested that if asymmetrical mitochondrial fission normally precedes mitophagy, then chronic suppression of fission by ablating Drp1 would have different consequences on <a href="https://qoto.org/tags/mitophagy" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitophagy</a> depending on when it is assayed.Mfn2 and PINK1–Parkin Mitophagy Signaling is a mechanism for controlling the quality of <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a> in the body. <a href="https://qoto.org/tags/PINK1" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#PINK1</a> and <a href="https://qoto.org/tags/Parkin" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#Parkin</a> are proteins that are linked to <a href="https://qoto.org/tags/Parkinson" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#Parkinson</a>'s disease, and mutations in their genes were the first to be identified as causing the disease. Scientists have studied how PINK1 interacts with Parkin, and how this interaction can lead to the destruction of damaged <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a>, which is called <a href="https://qoto.org/tags/mitophagy" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitophagy</a>. <a href="https://qoto.org/tags/PINK1" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#PINK1</a> is like an ignition switch that senses when mitochondrial damage has occurred, and then activates Parkin-mediated mitophagy. PINK1 is normally not present in healthy <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a>, but when mitochondrial damage occurs, PINK1 accumulates and triggers the destruction of the damaged <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a>.PINK1 is a protein that accumulates on damaged mitochondria and helps to promote mitophagy, which is the process of getting rid of damaged mitochondria. PINK1 does this by inducing the cytosolic protein Parkin to move to the mitochondria and ubiquitinate proteins on the outer membrane of the mitochondria. This helps to prevent the spread of damage from the damaged mitochondria to the healthy ones. PINK1 also inhibits the fusion of the damaged mitochondria. There are different theories about the biochemical events that cause Parkin to move to the mitochondria and stop the fusion. It is thought that PINK1 phosphorylates Parkin on certain sites, which helps Parkin bind to the mitochondria. It is also thought that PINK1 phosphorylates ubiquitin, which helps Parkin bind to the mitochondria and ubiquitinate proteins on the outer membrane. Finally, it is thought that PINK1 phosphorylates Mfn2, which helps Parkin bind to the mitochondria and ubiquitinate proteins on the outer membrane. All of these processes help to promote mitophagy and prevent the spread of damage from the damaged mitochondria to the healthy ones.<a href="https://qoto.org/tags/PINK1" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#PINK1</a> is a protein that plays an important role in a process called <a href="https://qoto.org/tags/mitophagy" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitophagy</a>, which is a form of quality control for mitochondria. Mutations in the <a href="https://qoto.org/tags/PINK1" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#PINK1</a> <a href="https://qoto.org/tags/gene" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#gene</a> have been linked to hereditary <a href="https://qoto.org/tags/Parkinson" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#Parkinson</a>'s disease in humans, but when the PINK1 gene is deleted in mice, it does not cause the same <a href="https://qoto.org/tags/neurodegenerative" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#neurodegenerative</a> pattern seen in humans. Even when the genes for PINK1, Parkin, and DJ-1 are all deleted in mice, it still does not cause the same loss of dopaminergic <a href="https://qoto.org/tags/neuron" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#neuron</a> s seen in <a href="https://qoto.org/tags/Parkinson" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#Parkinson</a>'s disease patients. This suggests that there may be other pathways that can compensate for the loss of <a href="https://qoto.org/tags/PINK1" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#PINK1</a> and <a href="https://qoto.org/tags/Parkin" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#Parkin</a>, such as increased transcription of other E3 <a href="https://qoto.org/tags/ubiquitin" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#ubiquitin</a> ligases in the hearts of Parkin-knockout mice.The text is discussing the idea of mitochondrial quality control pathways, which are processes that help keep mitochondria healthy. The text is suggesting that there may be alternate pathways that can be used to maintain mitochondrial health, rather than waiting until the mitochondria are completely depolarized before triggering their removal. It is comparing this idea to the idea of maintaining a car, where it is better to perform regular maintenance and repairs rather than waiting until the car is completely broken down before replacing it.Like a car, mitochondria can be maintained through preventative maintenance, such as replacing worn parts, and that more serious damage can be repaired by removing and replacing individual components. It also suggests that, like a car, <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a> can be repaired by removing and replacing damaged parts, but on a smaller scale. The different types of maintenance and repair may be part of a continuum, rather than distinct categories.<a href="https://qoto.org/tags/Mitophagy" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#Mitophagy</a> and mitochondrial dynamism are two processes that are closely connected. Mitophagy is the process of removing damaged <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a> from the <a href="https://qoto.org/tags/cell" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#cell</a>, while mitochondrial dynamism is the process of mitochondria fusing together and separating. The two processes work together to keep the cell healthy by eliminating damaged mitochondria and preventing healthy mitochondria from being contaminated by the damaged ones. The protein <a href="https://qoto.org/tags/Mfn2" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#Mfn2</a> plays a role in both processes, acting as a factor for mitochondrial fusion when it is not acted on by <a href="https://qoto.org/tags/PINK1" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#PINK1</a> and as a receptor for <a href="https://qoto.org/tags/Parkin" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#Parkin</a> when it is. This suggests that the two processes are mutually exclusive, meaning that they cannot happen at the same time. This helps to protect healthy <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a> from being contaminated by the damaged ones. Finally, the involvement of PINK1 and Parkin in multiple mitochondrial quality control mechanisms shows that there are multiple ways to keep the <a href="https://qoto.org/tags/mitochondria" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#mitochondria</a> healthy, which is important for preventing chronic degenerative diseases and providing opportunities for <a href="https://qoto.org/tags/therapeutic" class="mention hashtag" rel="nofollow noopener noreferrer" target="_blank">#therapeutic</a> intervention.

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