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Cellular and Molecular Life Sciences

, Volume 73, Issue 4, pp 775–795

First Online: 26 November 2015Received: 20 May 2015Revised: 30 October 2015Accepted: 02 November 2015DOI: 10.1007-s00018-015-2087-8

Cite this article as: Hamacher-Brady, A. & Brady, N.R. Cell. Mol. Life Sci. 2016 73: 775. doi:10.1007-s00018-015-2087-8

Abstract

Mitochondria are an essential source of ATP for cellular function, but when damaged, mitochondria generate a plethora of stress signals, which lead to cellular dysfunction and eventually programmed cell death. Thus, a major component of maintaining cellular homeostasis is the recognition and removal of dysfunctional mitochondria through autophagy-mediated degradation, i.e., mitophagy. Mitophagy further constitutes a developmental program, and undergoes a high degree of crosstalk with apoptosis. Reduced mitochondrial quality control is linked to disease pathogenesis, suggesting the importance of process elucidation as a clinical target. Recent work has revealed multiple mitophagy programs that operate independently or undergo crosstalk, and require modulated autophagy receptor activities at outer membranes of mitochondria. Here, we review these mitophagy programs, focusing on pathway mechanisms which recognize and target mitochondria for sequestration by autophagosomes, as well as mechanisms controlling pathway activities. Furthermore, we provide an introduction to the currently available methods for detecting mitophagy.

KeywordsBnip3 FUNDC1 LC3-interacting region LIR Macroautophagy Mitophagy Nix Parkin E3 ligase Ubiquitin AbbreviationsAtgAutophagy-related protein

GABARAPGamma-aminobutyric acid receptor-associated protein

HIF1Hypoxia-inducible factor 1

IMMInner mitochondrial membrane

LC3Microtubule-associated protein light chain 3

LIRLC3-interacting region

mTORMammalian target of rapamycin

OMMOuter mitochondrial membrane

PEPhosphatidylethanolamine

ROSReactive oxygen species

TCATricarboxylic acid

TFEBTranscription factor EB

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Autor: Anne Hamacher-Brady - Nathan Ryan Brady

Fuente: https://link.springer.com/







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