Global proximity interactome of the human ...
Document type :
Article dans une revue scientifique: Article original
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Title :
Global proximity interactome of the human macroautophagy pathway
Author(s) :
Tu, Yi Xin Iris [Auteur]
The Hospital for sick children [Toronto] [SickKids]
Sydor, Andrew M. [Auteur]
The Hospital for sick children [Toronto] [SickKids]
Coyaud, Etienne-Marie [Auteur]
Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192
Laurent, Estelle [Auteur]
Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192
Dyer, Diana [Auteur]
The Hospital for sick children [Toronto] [SickKids]
Mellouk, Nora [Auteur]
Dalhousie University [Halifax]
St-Germain, Jonathan R. [Auteur]
University Health Network [Toronto, ON, Canada]
Vernon, Robert M. [Auteur]
The Hospital for sick children [Toronto] [SickKids]
Forman-Kay, Julie D. [Auteur]
The Hospital for sick children [Toronto] [SickKids]
Li, Taoyingnan [Auteur]
The Hospital for sick children [Toronto] [SickKids]
Hua, Rong [Auteur]
The Hospital for sick children [Toronto] [SickKids]
Zhao, Kexin [Auteur]
Dalhousie University [Halifax]
Ridgway, Neale D. [Auteur]
The Hospital for sick children [Toronto] [SickKids]
Kim, Peter K. [Auteur]
The Hospital for sick children [Toronto] [SickKids]
Raught, Brian [Auteur]
The Hospital for sick children [Toronto] [SickKids]
Brumell, John H. [Auteur]
The Hospital for sick children [Toronto] [SickKids]
Department of Molecular Genetics [Toronto]
The Hospital for sick children [Toronto] [SickKids]
Sydor, Andrew M. [Auteur]
The Hospital for sick children [Toronto] [SickKids]
Coyaud, Etienne-Marie [Auteur]
Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192
Laurent, Estelle [Auteur]
Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192
Dyer, Diana [Auteur]
The Hospital for sick children [Toronto] [SickKids]
Mellouk, Nora [Auteur]
Dalhousie University [Halifax]
St-Germain, Jonathan R. [Auteur]
University Health Network [Toronto, ON, Canada]
Vernon, Robert M. [Auteur]
The Hospital for sick children [Toronto] [SickKids]
Forman-Kay, Julie D. [Auteur]
The Hospital for sick children [Toronto] [SickKids]
Li, Taoyingnan [Auteur]
The Hospital for sick children [Toronto] [SickKids]
Hua, Rong [Auteur]
The Hospital for sick children [Toronto] [SickKids]
Zhao, Kexin [Auteur]
Dalhousie University [Halifax]
Ridgway, Neale D. [Auteur]
The Hospital for sick children [Toronto] [SickKids]
Kim, Peter K. [Auteur]
The Hospital for sick children [Toronto] [SickKids]
Raught, Brian [Auteur]
The Hospital for sick children [Toronto] [SickKids]
Brumell, John H. [Auteur]
The Hospital for sick children [Toronto] [SickKids]
Department of Molecular Genetics [Toronto]
Journal title :
Autophagy
Abbreviated title :
Autophagy
Volume number :
18
Pages :
1-13
Publisher :
Taylor & Francis
Publication date :
2021-09-15
ISSN :
1554-8635
Keyword(s) :
OSBPL11
membrane contact site
lipid-transfer proteins
BioID
Salmonella
oxysterol-binding protein-like
OSBPL7
OSBPL
membrane contact site
lipid-transfer proteins
BioID
Salmonella
oxysterol-binding protein-like
OSBPL7
OSBPL
HAL domain(s) :
Sciences du Vivant [q-bio]
English abstract : [en]
Macroautophagy is a highly conserved eukaryotic cellular pathway involving the engulfment of macromolecules, organelles, and invading microbes by a double-membrane compartment and subsequent lysosomal degradation. The ...
Show more >Macroautophagy is a highly conserved eukaryotic cellular pathway involving the engulfment of macromolecules, organelles, and invading microbes by a double-membrane compartment and subsequent lysosomal degradation. The mechanisms that regulate macroautophagy, and the interaction of its components with other cellular pathways, have remained unclear. Here, we performed proximity-dependent biotin identification (BioID) on 39 core human macroautophagy proteins, identifying over 700 unique high confidence proximity interactors with new putative connections between macroautophagic and essential cellular processes. Of note, we identify members of the OSBPL (oxysterol binding protein like) family as Atg8-family protein interactors. We subsequently conducted comprehensive screens of the OSBPL family for LC3B-binding and roles in xenophagy and aggrephagy. OSBPL7 and OSBPL11 emerged as novel lipid transfer proteins required for macroautophagy of selective cargo. Altogether, our proximity interaction map provides a valuable resource for the study of autophagy and highlights the critical role of membrane contact site proteins in the pathway.Show less >
Show more >Macroautophagy is a highly conserved eukaryotic cellular pathway involving the engulfment of macromolecules, organelles, and invading microbes by a double-membrane compartment and subsequent lysosomal degradation. The mechanisms that regulate macroautophagy, and the interaction of its components with other cellular pathways, have remained unclear. Here, we performed proximity-dependent biotin identification (BioID) on 39 core human macroautophagy proteins, identifying over 700 unique high confidence proximity interactors with new putative connections between macroautophagic and essential cellular processes. Of note, we identify members of the OSBPL (oxysterol binding protein like) family as Atg8-family protein interactors. We subsequently conducted comprehensive screens of the OSBPL family for LC3B-binding and roles in xenophagy and aggrephagy. OSBPL7 and OSBPL11 emerged as novel lipid transfer proteins required for macroautophagy of selective cargo. Altogether, our proximity interaction map provides a valuable resource for the study of autophagy and highlights the critical role of membrane contact site proteins in the pathway.Show less >
Language :
Anglais
Audience :
Internationale
Popular science :
Non
Administrative institution(s) :
INSERM
Université de Lille
Université de Lille
Submission date :
2022-06-15T14:00:26Z
2023-04-12T06:59:31Z
2023-04-12T06:59:31Z
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