The dynamic nature of the K-Ras/calmodulin complex can be altered by oncogenic mutations.
Journal
Current opinion in structural biology
ISSN: 1879-033X
Titre abrégé: Curr Opin Struct Biol
Pays: England
ID NLM: 9107784
Informations de publication
Date de publication:
12 2021
12 2021
Historique:
received:
02
04
2021
revised:
03
06
2021
accepted:
17
06
2021
pubmed:
27
7
2021
medline:
15
12
2021
entrez:
26
7
2021
Statut:
ppublish
Résumé
Oncogenic mutant K-Ras promotes cancer cell proliferation, migration, invasion, and survival by assembling signaling complexes. To date, the functional and structural roles of K-Ras mutations within these complexes are incompletely understood despite their mechanistic and therapeutic significance. Here, we review recent advances in understanding specific binding between K-Ras and the calcium sensor calmodulin. This interaction positively and negatively regulates diverse functions of K-Ras in cancer, suggesting flexibility in K-Ras/calmodulin complex formation. Also, structural data suggest that oncogenic K-Ras likely samples several conformational states, influencing its distinct assemblies with calmodulin and with other proteins. Understanding how K-Ras interacts with calmodulin and with other partners is essential to discovering novel inhibitors of K-Ras in cancer.
Identifiants
pubmed: 34311289
pii: S0959-440X(21)00092-0
doi: 10.1016/j.sbi.2021.06.008
pii:
doi:
Substances chimiques
Calmodulin
0
Proto-Oncogene Proteins p21(ras)
EC 3.6.5.2
Calcium
SY7Q814VUP
Types de publication
Journal Article
Research Support, N.I.H., Intramural
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
164-170Subventions
Organisme : NCI NIH HHS
ID : R01 CA188427
Pays : United States
Organisme : NCI NIH HHS
ID : HHSN261200800001E
Pays : United States
Informations de copyright
Copyright © 2021 The Author(s). Published by Elsevier Ltd.. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest statement Nothing declared.