Autoinhibition of Sos by intramolecular interactions

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Article

Brian E. Hall², Shao-Song Yang³, Dafna Bar-Sagi^1,*

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¹ Department of Molecular Genetics and Microbiology, State University of New York at Stony Brook, Stony Brook, New York 11794-5222, USA

² The Graduate Programs in Molecular Pharmacology, State University of New York at Stony Brook, Stony Brook, New York 11794-5222, USA

³ Molecular and Cellular Biology, State University of New York at Stony Brook, Stony Brook, New York 11794-5222, USA

Front. Biosci. (Landmark Ed) 2002, 7(4), 288–294; https://doi.org/10.2741/hall

Published: 1 January 2002

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Abstract

Sos proteins function as activators of Ras signaling by catalyzing guanine nucleotide exchange on Ras. Sos regulation was initially thought to be accomplished primarily through its growth factor-dependent recruitment to the plasma membrane. More recent data has indicated that while membrane association is an indispensable means of Sos regulation, additional mechanisms involving intramolecular interactions function to control Sos activity towards Ras. This review will examine the experimental evidence for Sos intramolecular interactions and their contribution to Sos regulation.

Keywords

Ras

Sos

Autoinhibition

Receptor Tyrosine Kinase

Guanine Nucleotide Exchange

Intramolecular Interaction

Review

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