Defining bone fide effectors of RAS GTPases.
AFDN
PI3K
RAF
RAS GTPases
RBD domain
SCRIB
adherens junctions
Journal
BioEssays : news and reviews in molecular, cellular and developmental biology
ISSN: 1521-1878
Titre abrégé: Bioessays
Pays: United States
ID NLM: 8510851
Informations de publication
Date de publication:
09 2023
09 2023
Historique:
revised:
20
06
2023
received:
24
05
2023
accepted:
22
06
2023
medline:
28
8
2023
pubmed:
4
7
2023
entrez:
4
7
2023
Statut:
ppublish
Résumé
RAS GTPases play essential roles in normal development and are direct drivers of human cancers. Three decades of study have failed to wholly characterize pathways stimulated by activated RAS, driven by engagement with 'effector' proteins that have RAS binding domains (RBDs). Bone fide effectors must bind directly to RAS GTPases in a nucleotide-dependent manner, and this interaction must impart a clear change in effector activity. Despite this, for most proteins currently deemed effectors there is little mechanistic understanding of how binding to the GTPase alters protein function. There has also been limited effort to comprehensively resolve the specificity of effector binding to the full array of RAS superfamily GTPase proteins. This review will summarize what is known about RAS-driven activation for an array of potential effector proteins, focusing on structural and mechanistic effects and highlighting how little is still known regarding this key paradigm of cellular signal transduction.
Identifiants
pubmed: 37401638
doi: 10.1002/bies.202300088
doi:
Substances chimiques
ras Proteins
EC 3.6.5.2
Proteins
0
Nucleotides
0
Types de publication
Review
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2300088Informations de copyright
© 2023 The Authors. BioEssays published by Wiley Periodicals LLC.
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