NDLI: Interactome Analysis of the ER Stress Sensor Perk Uncovers Key Components of ER-Mitochondria Contact Sites and Ca2+ Signalling

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Interactome Analysis of the ER Stress Sensor Perk Uncovers Key Components of ER-Mitochondria Contact Sites and Ca2+ Signalling

Content Provider	SAGE Publishing
Author	Sassano, Maria Livia Derua, Rita Waelkens, Etienne Agostinis, Patrizia Alexander R van Vliet
Copyright Year	2021
Abstract	We recently reported that the ER stress kinase PERK regulates ER-mitochondria appositions and ER– plasma membrane (ER-PM) contact sites, independent of its canonical role in the unfolded protein response. PERK regulation of ER-PM contacts was revealed by a proximity biotinylation (BioID) approach and involved a dynamic PERK-Filamin A interaction supporting the formation of ER-PM contacts by actin-cytoskeleton remodeling in response to depletion of ER-Ca2+ stores. In this report, we further interrogated the PERK BioID interactome by validating through co-IP experiments the interaction between PERK and two proteins involved in Ca2+ handling and ER-mitochondria contact sites. These included the vesicle associated membrane (VAMP)-associated proteins (VAPA/B) and the main ER Ca2+ pump sarcoplasmic/endoplasmic reticulum Ca ATPase 2 (SERCA2). These data identify new putative PERK interacting proteins with a crucial role in membrane contact sites and Ca2+ signaling further supporting the uncanonical role of PERK in Ca2+ signaling through membrane contact sites (MCSs).
Related Links	https://journals.sagepub.com/doi/pdf/10.1177/25152564211052392?download=true
ISSN	25152564
Volume Number	4
Journal	Contact (CTC)
e-ISSN	25152564
DOI	10.1177/25152564211052392
Language	English
Publisher	Sage Publications CA
Publisher Date	2021-11-29
Publisher Place	Los Angeles
Access Restriction	Open
Rights Holder	© The Author(s) 2021
Subject Keyword	mitochondrial associated membranes (MAM) ER stress cell biology sarco/endoplasmic reticulum Ca2+-ATPase (SERCA) endoplasmic reticulum
Content Type	Text
Resource Type	Article

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