Sticking With It: ER-PM Membrane Contact Sites as a Coordinating Nexus for Regulating Lipids and Proteins at the Cell Cortex.
ER-PM contact sites
VAP (VAMP-associated protein)
endoplasmic reticulum
extended synaptotagmins
membrane stress
membrane tethers
phospholipid regulation
plasma membrane
Journal
Frontiers in cell and developmental biology
ISSN: 2296-634X
Titre abrégé: Front Cell Dev Biol
Pays: Switzerland
ID NLM: 101630250
Informations de publication
Date de publication:
2020
2020
Historique:
received:
17
04
2020
accepted:
03
07
2020
entrez:
15
8
2020
pubmed:
15
8
2020
medline:
15
8
2020
Statut:
epublish
Résumé
Membrane contact sites between the cortical endoplasmic reticulum (ER) and the plasma membrane (PM) provide a direct conduit for small molecule transfer and signaling between the two largest membranes of the cell. Contact is established through ER integral membrane proteins that physically tether the two membranes together, though the general mechanism is remarkably non-specific given the diversity of different tethering proteins. Primary tethers including VAMP-associated proteins (VAPs), Anoctamin/TMEM16/Ist2p homologs, and extended synaptotagmins (E-Syts), are largely conserved in most eukaryotes and are both necessary and sufficient for establishing ER-PM association. In addition, other species-specific ER-PM tether proteins impart unique functional attributes to both membranes at the cell cortex. This review distils recent functional and structural findings about conserved and species-specific tethers that form ER-PM contact sites, with an emphasis on their roles in the coordinate regulation of lipid metabolism, cellular structure, and responses to membrane stress.
Identifiants
pubmed: 32793605
doi: 10.3389/fcell.2020.00675
pmc: PMC7387695
doi:
Types de publication
Journal Article
Review
Langues
eng
Pagination
675Informations de copyright
Copyright © 2020 Zaman, Nenadic, Radojičić, Rosado and Beh.
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