VIPP1 rods engulf membranes containing phosphatidylinositol phosphates.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
19 06 2019
19 06 2019
Historique:
received:
27
10
2018
accepted:
14
05
2019
entrez:
21
6
2019
pubmed:
21
6
2019
medline:
21
10
2020
Statut:
epublish
Résumé
In cyanobacteria and plants, VIPP1 plays crucial roles in the biogenesis and repair of thylakoid membrane protein complexes and in coping with chloroplast membrane stress. In chloroplasts, VIPP1 localizes in distinct patterns at or close to envelope and thylakoid membranes. In vitro, VIPP1 forms higher-order oligomers of >1 MDa that organize into rings and rods. However, it remains unknown how VIPP1 oligomerization is related to function. Using time-resolved fluorescence anisotropy and sucrose density gradient centrifugation, we show here that Chlamydomonas reinhardtii VIPP1 binds strongly to liposomal membranes containing phosphatidylinositol-4-phosphate (PI4P). Cryo-electron tomography reveals that VIPP1 oligomerizes into rods that can engulf liposomal membranes containing PI4P. These findings place VIPP1 into a group of membrane-shaping proteins including epsin and BAR domain proteins. Moreover, they point to a potential role of phosphatidylinositols in directing the shaping of chloroplast membranes.
Identifiants
pubmed: 31217458
doi: 10.1038/s41598-019-44259-3
pii: 10.1038/s41598-019-44259-3
pmc: PMC6584618
doi:
Substances chimiques
Membrane Proteins
0
Membranes, Artificial
0
Phosphatidylinositol Phosphates
0
Plant Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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