Golgi-derived PI


Journal

Science (New York, N.Y.)
ISSN: 1095-9203
Titre abrégé: Science
Pays: United States
ID NLM: 0404511

Informations de publication

Date de publication:
20 03 2020
Historique:
received: 09 04 2019
revised: 09 12 2019
accepted: 27 02 2020
entrez: 21 3 2020
pubmed: 21 3 2020
medline: 25 3 2020
Statut: ppublish

Résumé

Mitochondrial plasticity is a key regulator of cell fate decisions. Mitochondrial division involves Dynamin-related protein-1 (Drp1) oligomerization, which constricts membranes at endoplasmic reticulum (ER) contact sites. The mechanisms driving the final steps of mitochondrial division are still unclear. Here, we found that microdomains of phosphatidylinositol 4-phosphate [PI(4)P] on trans-Golgi network (TGN) vesicles were recruited to mitochondria-ER contact sites and could drive mitochondrial division downstream of Drp1. The loss of the small guanosine triphosphatase ADP-ribosylation factor 1 (Arf1) or its effector, phosphatidylinositol 4-kinase IIIβ [PI(4)KIIIβ], in different mammalian cell lines prevented PI(4)P generation and led to a hyperfused and branched mitochondrial network marked with extended mitochondrial constriction sites. Thus, recruitment of TGN-PI(4)P-containing vesicles at mitochondria-ER contact sites may trigger final events leading to mitochondrial scission.

Identifiants

pubmed: 32193326
pii: 367/6484/1366
doi: 10.1126/science.aax6089
doi:

Substances chimiques

Phosphatidylinositol Phosphates 0
phosphatidylinositol 4-phosphate 0
1-Phosphatidylinositol 4-Kinase EC 2.7.1.67
ADP-Ribosylation Factor 1 EC 3.6.5.2
ARF1 protein, human EC 3.6.5.2
DNM1L protein, human EC 3.6.5.5
Dynamins EC 3.6.5.5

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1366-1371

Subventions

Organisme : Medical Research Council
ID : MC_UU_00015/7
Pays : United Kingdom
Organisme : Wellcome Trust
Pays : United Kingdom

Commentaires et corrections

Type : CommentIn

Informations de copyright

Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.

Auteurs

Shun Nagashima (S)

Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge CB2 0XY, UK.

Luis-Carlos Tábara (LC)

Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge CB2 0XY, UK.

Lisa Tilokani (L)

Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge CB2 0XY, UK.

Vincent Paupe (V)

Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge CB2 0XY, UK.

Hanish Anand (H)

Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge CB2 0XY, UK.

Joe H Pogson (JH)

Department of Neurology and Neurosurgery, McGill University, Montreal, Quebec H3B 2B4, Canada.

Rodolfo Zunino (R)

Department of Neurology and Neurosurgery, McGill University, Montreal, Quebec H3B 2B4, Canada.

Heidi M McBride (HM)

Department of Neurology and Neurosurgery, McGill University, Montreal, Quebec H3B 2B4, Canada. heidi.mcbride@mcgill.ca julien.prudent@mrc-mbu.cam.ac.uk.

Julien Prudent (J)

Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge CB2 0XY, UK. heidi.mcbride@mcgill.ca julien.prudent@mrc-mbu.cam.ac.uk.

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Classifications MeSH