Plasma membrane tethering of the cortical ER necessitates its finely reticulated architecture.

Détails

ID Serval
serval:BIB_DEE3377500EE
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Plasma membrane tethering of the cortical ER necessitates its finely reticulated architecture.
Périodique
Current biology
Auteur(s)
Zhang D., Vjestica A., Oliferenko S.
ISSN
1879-0445 (Electronic)
ISSN-L
0960-9822
Statut éditorial
Publié
Date de publication
06/11/2012
Peer-reviewed
Oui
Volume
22
Numéro
21
Pages
2048-2052
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
The cortical endoplasmic reticulum (ER) is an intricate network of tubules and cisternae tightly associated with the plasma membrane (PM) in plants, yeast, and the excitable cell types in metazoans [1-5]. How the ER is attached to the cell cortex and what necessitates its highly reticulated architecture remain largely unknown. Here, we identify the integral ER vesicle-associated membrane protein-associated proteins (VAPs), previously shown to control the composition of phosphoinositides at the ER-PM contact sites [6, 7], as major players in sustaining the ER-PM tethering in fission yeast. We show that genetic conversion of the reticulated ER structure to the cisternal morphology shields large areas of the PM, preventing the actomyosin division ring assembly at the equatorial cortex. Using a combination of VAP mutants where the cortical ER is detached from the PM and a set of artificial ER-PM tethers suppressing this phenotype, we demonstrate that the PM footprint of the cortical ER is functionally insulated from the cytosol. In cells with prominent ER-PM contacts, fine reticulation of the ER network may have emerged as a critical adaptation enabling a uniform access of peripheral protein complexes to the inner surface of the plasma membrane.
Mots-clé
Actomyosin/metabolism, Cell Division, Cell Membrane/metabolism, Cell Membrane/ultrastructure, Endoplasmic Reticulum/metabolism, Endoplasmic Reticulum/ultrastructure, Mutation, Phosphatidylinositols/metabolism, R-SNARE Proteins/genetics, R-SNARE Proteins/metabolism, Schizosaccharomyces/genetics, Schizosaccharomyces/metabolism, Schizosaccharomyces/ultrastructure, Schizosaccharomyces pombe Proteins/genetics, Schizosaccharomyces pombe Proteins/metabolism
Pubmed
Web of science
Open Access
Oui
Création de la notice
13/01/2021 16:52
Dernière modification de la notice
20/01/2021 7:26
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