CALCOCO1 acts with VAMP-associated proteins to mediate ER-phagy.
FFAT
VAPA
Autophagy
CALCOCO1
ER-phagy
Journal
The EMBO journal
ISSN: 1460-2075
Titre abrégé: EMBO J
Pays: England
ID NLM: 8208664
Informations de publication
Date de publication:
03 08 2020
03 08 2020
Historique:
received:
07
10
2019
revised:
01
05
2020
accepted:
06
05
2020
pubmed:
12
6
2020
medline:
10
4
2021
entrez:
12
6
2020
Statut:
ppublish
Résumé
The endoplasmic reticulum (ER) plays important roles in protein synthesis and folding, and calcium storage. The volume of the ER and expression of its resident proteins are increased in response to nutrient stress. ER-phagy, a selective form of autophagy, is involved in the degradation of the excess components of the ER to restore homeostasis. Six ER-resident proteins have been identified as ER-phagy receptors so far. In this study, we have identified CALCOCO1 as a novel ER-phagy receptor for the degradation of the tubular ER in response to proteotoxic and nutrient stress. CALCOCO1 is a homomeric protein that binds directly to ATG8 proteins via LIR- and UDS-interacting region (UIR) motifs acting co-dependently. CALCOCO1-mediated ER-phagy requires interaction with VAMP-associated proteins VAPA and VAPB on the ER membranes via a conserved FFAT-like motif. Depletion of CALCOCO1 causes expansion of the ER and inefficient basal autophagy flux. Unlike the other ER-phagy receptors, CALCOCO1 is peripherally associated with the ER. Therefore, we define CALCOCO1 as a soluble ER-phagy receptor.
Identifiants
pubmed: 32525583
doi: 10.15252/embj.2019103649
pmc: PMC7396842
doi:
Substances chimiques
CALCOCO1 protein, human
0
Calcium-Binding Proteins
0
Calcoco1 protein, mouse
0
Transcription Factors
0
VAPA protein, human
0
VAPB protein, human
0
VAPB protein, mouse
0
Vapa protein, mouse
0
Vesicular Transport Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e103649Subventions
Organisme : Norges Forskningsråd (Forskningsrådet)
ID : 214448
Organisme : Norges Forskningsråd (Forskningsrådet)
ID : 249884
Informations de copyright
© 2020 The Authors. Published under the terms of the CC BY 4.0 license.
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