ER-associated VAP27-1 and VAP27-3 proteins functionally link the lipid-binding ORP2A at the ER-chlor...
ER-associated VAP27-1 and VAP27-3 proteins functionally link the lipid-binding ORP2A at the ER-chloroplast contact sites
About this item
Full title
Author / Creator
Renna, Luciana , Stefano, Giovanni , Puggioni, Maria Paola , Kim, Sang-Jin , Lavell, Anastasiya , Froehlich, John E. , Burkart, Graham , Mancuso, Stefano , Benning, Christoph , Brandizzi, Federica , Michigan State Univ., East Lansing, MI (United States) and Univ. of Wisconsin, Madison, WI (United States)
Publisher
London: Nature Publishing Group UK
Journal title
Language
English
Formats
Publication information
Publisher
London: Nature Publishing Group UK
Subjects
More information
Scope and Contents
Contents
The plant endoplasmic reticulum (ER) contacts heterotypic membranes at membrane contact sites (MCSs) through largely undefined mechanisms. For instance, despite the well-established and essential role of the plant ER-chloroplast interactions for lipid biosynthesis, and the reported existence of physical contacts between these organelles, almost not...
Alternative Titles
Full title
ER-associated VAP27-1 and VAP27-3 proteins functionally link the lipid-binding ORP2A at the ER-chloroplast contact sites
Authors, Artists and Contributors
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_doaj_primary_oai_doaj_org_article_d59a0efc734a475fb346c87f4343e84f
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_d59a0efc734a475fb346c87f4343e84f
Other Identifiers
ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-024-50425-7
