FERM domains recruit ample PI(4,5)P
Journal
Biophysical journal
ISSN: 1542-0086
Titre abrégé: Biophys J
Pays: United States
ID NLM: 0370626
Informations de publication
Date de publication:
04 04 2023
04 04 2023
Historique:
received:
29
10
2022
revised:
26
01
2023
accepted:
18
02
2023
pmc-release:
04
04
2024
medline:
7
4
2023
pubmed:
24
2
2023
entrez:
23
2
2023
Statut:
ppublish
Résumé
The four-point-one ezrin-radixin-moesin homology (FERM) protein domain is a multifunctional protein-lipid binding site, constituting an integral part of numerous membrane-associated proteins. Its interaction with the lipid phosphatidylinositol-4,5-bisphosphate (PIP
Identifiants
pubmed: 36814382
pii: S0006-3495(23)00133-9
doi: 10.1016/j.bpj.2023.02.027
pmc: PMC10111351
pii:
doi:
Substances chimiques
Lipid Bilayers
0
Focal Adhesion Protein-Tyrosine Kinases
EC 2.7.10.2
Phosphatidylinositol 4,5-Diphosphate
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1325-1333Informations de copyright
Copyright © 2023 Biophysical Society. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests The authors declare no competing interests.
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