Difference between revisions of "Mitophagy"
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| | |description=Autophagy (self-eating) in general is viewed as a degradation process which removes non-essential or damaged cellular constituents. | ||
» [[Mitophagy#Mitochondrial_mitophagy | '''MiPNet article''']] | |||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/21868666 Green_2011_Science] | |info=[http://www.ncbi.nlm.nih.gov/pubmed/21868666 Green_2011_Science] | ||
}} | }} | ||
{{MitoPedia methods | {{MitoPedia concepts}} | ||
| | {{MitoPedia methods}} | ||
{{MitoPedia O2k and high-resolution respirometry}} | |||
{{MitoPedia topics}} | |||
__TOC__ | |||
= Mitochondrial mitophagy = | |||
{{Publication | |||
|title=Pesta D (2012) Mitochondrial mitophagy. Mitochondr Physiol Network 2012-05-22. | |||
|info= | |||
|authors=Pesta D | |||
|year=2012 | |||
|journal=MiPNet | |||
|abstract=A brief accout of '''mitochondrial mitophagy'''. | |||
|mipnetlab=AT Innsbruck Gnaiger E, DE Cologne Pesta D | |||
}} | |||
{{Labeling | |||
|area=mt-Structure;fission;fusion | |||
|instruments=Theory | |||
}} | }} | ||
== Mechanism == | |||
'''Mitophagy''', which is specifically targeted to mitochondria, eliminates dysfunctional or damaged mitochondria. During the course of life, mitochondrial genomes accumulate mutations that impair respiration and can lead to excessive formation of [[reactive oxygen species]] (ROS). ROS is also a well-known side product of normal [[respiration]] and can damage other organelles. By eliminating damaged or dysfunctional components of the cell and the mitochondrion, mitophagy is an important mechanism in the cellular adaptation to stress and serves as a quality-control ensuring proper mitochondrial and cell function. | |||
== Definition == | |||
Autophagy, or in mitochondrial terms, mitophagy occurs by the formation of autophagosomes. These essentially double-membraned vesicles sequester damaged organelles, proteins, or portions of the cytoplasm, which then fuse with lysosomes. After being fused, the sequestered contents are degraded by the acidic environment of lysosomal enzymes. In order to accomplish this task, more than 30 Atg (AuTophaGy-related) proteins are recruited. | Autophagy, or in mitochondrial terms, mitophagy occurs by the formation of autophagosomes. These essentially double-membraned vesicles sequester damaged organelles, proteins, or portions of the cytoplasm, which then fuse with lysosomes. After being fused, the sequestered contents are degraded by the acidic environment of lysosomal enzymes. In order to accomplish this task, more than 30 Atg (AuTophaGy-related) proteins are recruited. | ||
Latest revision as of 10:11, 23 May 2022
- high-resolution terminology - matching measurements at high-resolution
Mitophagy
Description
Autophagy (self-eating) in general is viewed as a degradation process which removes non-essential or damaged cellular constituents. » MiPNet article
Reference: Green_2011_Science
Mitochondrial mitophagy
| Pesta D (2012) Mitochondrial mitophagy. Mitochondr Physiol Network 2012-05-22. |
Abstract: A brief accout of mitochondrial mitophagy.
• O2k-Network Lab: AT Innsbruck Gnaiger E, DE Cologne Pesta D
Labels: MiParea: mt-Structure;fission;fusion
HRR: Theory
Mechanism
Mitophagy, which is specifically targeted to mitochondria, eliminates dysfunctional or damaged mitochondria. During the course of life, mitochondrial genomes accumulate mutations that impair respiration and can lead to excessive formation of reactive oxygen species (ROS). ROS is also a well-known side product of normal respiration and can damage other organelles. By eliminating damaged or dysfunctional components of the cell and the mitochondrion, mitophagy is an important mechanism in the cellular adaptation to stress and serves as a quality-control ensuring proper mitochondrial and cell function.
Definition
Autophagy, or in mitochondrial terms, mitophagy occurs by the formation of autophagosomes. These essentially double-membraned vesicles sequester damaged organelles, proteins, or portions of the cytoplasm, which then fuse with lysosomes. After being fused, the sequestered contents are degraded by the acidic environment of lysosomal enzymes. In order to accomplish this task, more than 30 Atg (AuTophaGy-related) proteins are recruited.
