Rab7b modulates autophagic flux by interacting with Atg4B

Kjos, Ingrid, Borg Distefano, Marita, Sætre, Frank, Repnik, Urska, Holland, Petter, Jones, Arwyn T. ORCID: https://orcid.org/0000-0003-2781-8905, Engedal, Nikolai, Simonsen, Anne, Bakke, Oddmund and Progida, Cinzia 2017. Rab7b modulates autophagic flux by interacting with Atg4B. EMBO reports 18 (10) , pp. 1727-1739. 10.15252/embr.201744069

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Abstract

Autophagy (macroautophagy) is a highly conserved eukaryotic degradation pathway in which cytosolic components and organelles are sequestered by specialized autophagic membranes and degraded through the lysosomal system. The autophagic pathway maintains basal cellular homeostasis and helps cells adapt during stress; thus, defects in autophagy can cause detrimental effects. It is therefore crucial that autophagy is properly regulated. In this study, we show that the cysteine protease Atg4B, a key enzyme in autophagy that cleaves LC3, is an interactor of the small GTPase Rab7b. Indeed, Atg4B interacts and co‐localizes with Rab7b on vesicles. Depletion of Rab7b increases autophagic flux as indicated by the increased size of autophagic structures as well as the magnitude of macroautophagic sequestration and degradation. Importantly, we demonstrate that Rab7b regulates LC3 processing by modulating Atg4B activity. Taken together, our findings reveal Rab7b as a novel negative regulator of autophagy through its interaction with Atg4B.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Pharmacy
Additional Information:	This is an open access article under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License
Publisher:	EMBO Press
ISSN:	1469-221X
Date of First Compliant Deposit:	30 August 2017
Date of Acceptance:	29 June 2017
Last Modified:	02 May 2023 15:48
URI:	https://orca.cardiff.ac.uk/id/eprint/104100

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