Ontology highlight
ABSTRACT:
SUBMITTER: Young LC
PROVIDER: S-EPMC6233131 | biostudies-literature | 2018 Nov
REPOSITORIES: biostudies-literature
Young Lucy C LC Hartig Nicole N Boned Del Río Isabel I Sari Sibel S Ringham-Terry Benjamin B Wainwright Joshua R JR Jones Greg G GG McCormick Frank F Rodriguez-Viciana Pablo P
Proceedings of the National Academy of Sciences of the United States of America 20181022 45
Dephosphorylation of the inhibitory "S259" site on RAF kinases (S259 on CRAF, S365 on BRAF) plays a key role in RAF activation. The MRAS GTPase, a close relative of RAS oncoproteins, interacts with SHOC2 and protein phosphatase 1 (PP1) to form a heterotrimeric holoenzyme that dephosphorylates this S259 RAF site. MRAS and SHOC2 function as PP1 regulatory subunits providing the complex with striking specificity against RAF. MRAS also functions as a targeting subunit as membrane localization is req ...[more]