<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Palikaras, K.</style></author><author><style face="normal" font="default" size="100%">Lionaki, E.</style></author><author><style face="normal" font="default" size="100%">Tavernarakis, N.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Coupling mitogenesis and mitophagy for longevity</style></title><secondary-title><style face="normal" font="default" size="100%">Autophagy</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">*Autophagy</style></keyword><keyword><style  face="normal" font="default" size="100%">*Mitophagy</style></keyword><keyword><style  face="normal" font="default" size="100%">Aging</style></keyword><keyword><style  face="normal" font="default" size="100%">Aging/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Autophagy</style></keyword><keyword><style  face="normal" font="default" size="100%">Caenorhabditis elegans</style></keyword><keyword><style  face="normal" font="default" size="100%">Caenorhabditis elegans Proteins/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Caenorhabditis elegans/*physiology</style></keyword><keyword><style  face="normal" font="default" size="100%">Carrier Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA-Binding Proteins/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">homeostasis</style></keyword><keyword><style  face="normal" font="default" size="100%">Longevity</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane Proteins/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Mitochondria</style></keyword><keyword><style  face="normal" font="default" size="100%">Mitochondria/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">mitophagy</style></keyword><keyword><style  face="normal" font="default" size="100%">signal transduction</style></keyword><keyword><style  face="normal" font="default" size="100%">stress</style></keyword><keyword><style  face="normal" font="default" size="100%">Transcription Factors/metabolism</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2015</style></year></dates><number><style face="normal" font="default" size="100%">8</style></number><edition><style face="normal" font="default" size="100%">2015/06/18</style></edition><volume><style face="normal" font="default" size="100%">11</style></volume><pages><style face="normal" font="default" size="100%">1428-30</style></pages><isbn><style face="normal" font="default" size="100%">1554-8635 (Electronic)1554-8627 (Linking)</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Maintenance of mitochondrial function and energy homeostasis requires both generation of newly synthesized and elimination of dysfunctional mitochondria. Impaired mitochondrial function and excessive mitochondrial content are major characteristics of aging and several human pathophysiological conditions, highlighting the pivotal role of the coordination between mitochondrial biogenesis and mitophagy. However, the cellular and molecular underpinnings of mitochondrial mass homeostasis remain obscure. In our recent study, we demonstrate that DCT-1, the Caenorhabditis elegans homolog of mammalian BNIP3 and BNIP3L/NIX, is a key mediator of mitophagy promoting longevity under stress. DCT-1 acts downstream of the PINK-1-PDR-1/Parkin pathway and is ubiquitinated upon mitophagy-inducing conditions to mediate the removal of damaged mitochondria. Accumulation of damaged mitochondria triggers SKN-1 activation, which initiates a bipartite retrograde signaling pathway stimulating the coordinated induction of both mitochondrial biogenesis and mitophagy genes. Taken together, our results unravel a homeostatic feedback loop that allows cells to adjust their mitochondrial population in response to environmental and intracellular cues. Age-dependent decline of mitophagy both inhibits removal of dysfunctional or superfluous mitochondria and impairs mitochondrial biogenesis resulting in progressive mitochondrial accretion and consequently, deterioration of cell function.</style></abstract><accession-num><style face="normal" font="default" size="100%">26083448</style></accession-num><notes><style face="normal" font="default" size="100%">Palikaras, KonstantinosLionaki, EiriniTavernarakis, NektariosengResearch Support, Non-U.S. Gov'tAutophagy. 2015;11(8):1428-30. doi: 10.1080/15548627.2015.1061172.</style></notes><custom2><style face="normal" font="default" size="100%">PMC4590656</style></custom2><auth-address><style face="normal" font="default" size="100%">a Institute of Molecular Biology and Biotechnology; Foundation for Research and Technology-Hellas ; Heraklion , Crete , Greece.</style></auth-address></record></records></xml>