NDLI: The ER-localized autophagy protein EPG-3/VMP1 regulates ER contacts with other organelles by modulating ATP2A/SERCA activity

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The ER-localized autophagy protein EPG-3/VMP1 regulates ER contacts with other organelles by modulating ATP2A/SERCA activity

Content Provider	Scilit
Author	Zhao, Yan G. Zhang, Hong
Copyright Year	2018
Description	The ER forms contacts with other endomembrane systems to exchange materials (e.g., calcium and lipids) and also to modulate dynamic organelle processes, including fission, cargo sorting and movement. During autophagosome formation, dynamic contacts between the ER and the phagophore membrane are crucial for phagophore expansion and closure. Little is known about the mechanisms underlying the formation and disassembly of the ER contacts. We found that the ER-localized autophagy protein EPG-3/VMP1 plays an essential role in controlling ER-phagophore dissociation and also the disassembly of ER contacts with LDs, mitochondria and endolysosomes. VMP1 regulates the ER contact by activating the ER calcium channel ATP2A/SERCA (ATPase sarcoplasmic/endoplasmic reticulum Ca2+ transporting). CALM (calmodulin) acts as one of the downstream calcium effectors that controls the PIK3C3/VPS34 phosphatidylinositol (PtdIns) 3-kinase (PtdIns3K) activity to maintain these contacts. Our study provides insights into the molecular mechanisms which regulate ER contacts and generate autophagosomes.
Related Links	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5902242/pdf
Ending Page	363
Page Count	2
Starting Page	362
ISSN	15548627
e-ISSN	15548635
DOI	10.1080/15548627.2017.1415591
Journal	Autophagy
Issue Number	2
Volume Number	14
Language	English
Publisher	Informa UK Limited
Publisher Date	2018-02-01
Access Restriction	Open
Subject Keyword	Journal: Autophagy Cell Biology Membrane Contact Organelle Serca Vmp1
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology

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