ATG2 regulation of phagophore expansion at mitochondria-associated ER membranes

Research output: Contribution to journalComment/debate

Abstract

The mechanism by which ATG2 (ATG2A and ATG2B in mammals) regulates autophagosome biogenesis remains largely unknown. In our recent study, we showed that ATG2A translocates to the mitochondria-associated ER membranes (MAM) to promote phagophore growth during nutrient starvation. Mechanistically, the mitochondrial translocase TOMM40 binds to a C-terminal domain of ATG2A, termed the MAM localization domain (MLD), and mediates its MAM translocation in a manner dependent on the TOMM receptor TOMM70. Moreover, ATG2A associates with ATG9A through its N-terminal domain and this interaction is required for phagophore expansion and efficient autophagic flux. These observations suggest that ATG2 operates a mechanism for phagophore expansion at the MAM through the TOMM40-TOMM70 complex and ATG9 during autophagy.

Original languageEnglish (US)
Pages (from-to)2165-2166
Number of pages2
JournalAutophagy
Volume15
Issue number12
DOIs
StatePublished - Dec 2 2019

Fingerprint

Mitochondria
Membranes
Autophagy
Starvation
Mammals
Food
Growth

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

Cite this

@article{64192580f6f54c268875e092fb80ec3b,
title = "ATG2 regulation of phagophore expansion at mitochondria-associated ER membranes",
abstract = "The mechanism by which ATG2 (ATG2A and ATG2B in mammals) regulates autophagosome biogenesis remains largely unknown. In our recent study, we showed that ATG2A translocates to the mitochondria-associated ER membranes (MAM) to promote phagophore growth during nutrient starvation. Mechanistically, the mitochondrial translocase TOMM40 binds to a C-terminal domain of ATG2A, termed the MAM localization domain (MLD), and mediates its MAM translocation in a manner dependent on the TOMM receptor TOMM70. Moreover, ATG2A associates with ATG9A through its N-terminal domain and this interaction is required for phagophore expansion and efficient autophagic flux. These observations suggest that ATG2 operates a mechanism for phagophore expansion at the MAM through the TOMM40-TOMM70 complex and ATG9 during autophagy.",
author = "Zhenyuan Tang and Yoshinori Takahashi and Wang, {Hong Gang}",
year = "2019",
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language = "English (US)",
volume = "15",
pages = "2165--2166",
journal = "Autophagy",
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ATG2 regulation of phagophore expansion at mitochondria-associated ER membranes. / Tang, Zhenyuan; Takahashi, Yoshinori; Wang, Hong Gang.

In: Autophagy, Vol. 15, No. 12, 02.12.2019, p. 2165-2166.

Research output: Contribution to journalComment/debate

TY - JOUR

T1 - ATG2 regulation of phagophore expansion at mitochondria-associated ER membranes

AU - Tang, Zhenyuan

AU - Takahashi, Yoshinori

AU - Wang, Hong Gang

PY - 2019/12/2

Y1 - 2019/12/2

N2 - The mechanism by which ATG2 (ATG2A and ATG2B in mammals) regulates autophagosome biogenesis remains largely unknown. In our recent study, we showed that ATG2A translocates to the mitochondria-associated ER membranes (MAM) to promote phagophore growth during nutrient starvation. Mechanistically, the mitochondrial translocase TOMM40 binds to a C-terminal domain of ATG2A, termed the MAM localization domain (MLD), and mediates its MAM translocation in a manner dependent on the TOMM receptor TOMM70. Moreover, ATG2A associates with ATG9A through its N-terminal domain and this interaction is required for phagophore expansion and efficient autophagic flux. These observations suggest that ATG2 operates a mechanism for phagophore expansion at the MAM through the TOMM40-TOMM70 complex and ATG9 during autophagy.

AB - The mechanism by which ATG2 (ATG2A and ATG2B in mammals) regulates autophagosome biogenesis remains largely unknown. In our recent study, we showed that ATG2A translocates to the mitochondria-associated ER membranes (MAM) to promote phagophore growth during nutrient starvation. Mechanistically, the mitochondrial translocase TOMM40 binds to a C-terminal domain of ATG2A, termed the MAM localization domain (MLD), and mediates its MAM translocation in a manner dependent on the TOMM receptor TOMM70. Moreover, ATG2A associates with ATG9A through its N-terminal domain and this interaction is required for phagophore expansion and efficient autophagic flux. These observations suggest that ATG2 operates a mechanism for phagophore expansion at the MAM through the TOMM40-TOMM70 complex and ATG9 during autophagy.

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