Redefining the specificity of phosphoinositide-binding by human PH domain-containing proteins.
Algorithms
Animals
Binding Sites
Computational Biology
/ methods
HEK293 Cells
Humans
Mice
Microscopy, Fluorescence
NIH 3T3 Cells
Phosphatidylinositols
/ chemistry
Phosphatidylserines
/ chemistry
Pleckstrin Homology Domains
Proteins
/ chemistry
Rho Guanine Nucleotide Exchange Factors
/ chemistry
Sensitivity and Specificity
rhoA GTP-Binding Protein
/ metabolism
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
15 07 2021
15 07 2021
Historique:
received:
25
11
2020
accepted:
18
06
2021
entrez:
16
7
2021
pubmed:
17
7
2021
medline:
31
7
2021
Statut:
epublish
Résumé
Pleckstrin homology (PH) domains are presumed to bind phosphoinositides (PIPs), but specific interaction with and regulation by PIPs for most PH domain-containing proteins are unclear. Here we employ a single-molecule pulldown assay to study interactions of lipid vesicles with full-length proteins in mammalian whole cell lysates. Of 67 human PH domain-containing proteins initially examined, 36 (54%) are found to have affinity for PIPs with various specificity, the majority of which have not been reported before. Further investigation of ARHGEF3 reveals distinct structural requirements for its binding to PI(4,5)P
Identifiants
pubmed: 34267198
doi: 10.1038/s41467-021-24639-y
pii: 10.1038/s41467-021-24639-y
pmc: PMC8282632
doi:
Substances chimiques
ARHGEF3 protein, human
0
Phosphatidylinositols
0
Phosphatidylserines
0
Proteins
0
Rho Guanine Nucleotide Exchange Factors
0
rhoA GTP-Binding Protein
EC 3.6.5.2
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4339Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM089771
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM122569
Pays : United States
Organisme : Howard Hughes Medical Institute
Pays : United States
Informations de copyright
© 2021. The Author(s).
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