Mechanism of SOS PR-domain autoinhibition revealed by single-molecule assays on native protein from lysate

Young Kwang Lee; Shalini T. Low-Nam; Jean K. Chung; Scott D. Hansen; Hiu Yue Monatrice Lam; Steven Alvarez; Jay T. Groves

doi:10.1038/ncomms15061

Nature Communications (Apr 2017)

Mechanism of SOS PR-domain autoinhibition revealed by single-molecule assays on native protein from lysate

Young Kwang Lee,
Shalini T. Low-Nam,
Jean K. Chung,
Scott D. Hansen,
Hiu Yue Monatrice Lam,
Steven Alvarez,
Jay T. Groves

Affiliations

Young Kwang Lee: Department of Chemistry, University of California
Shalini T. Low-Nam: Department of Chemistry, University of California
Jean K. Chung: Department of Chemistry, University of California
Scott D. Hansen: Department of Chemistry, University of California
Hiu Yue Monatrice Lam: Department of Chemistry, University of California
Steven Alvarez: Department of Chemistry, University of California
Jay T. Groves: Department of Chemistry, University of California

DOI: https://doi.org/10.1038/ncomms15061
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 11

Abstract

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The guanine nucleotide exchange factor SOS is a critical intermediary that transduces receptor tyrosine kinase stimulation into Ras activation. Here the authors develop a single molecule assay in which SOS is captured from raw lysates using Ras-functionalized membrane microarrays and uncover an autoinhibitory mechanism of SOS regulation.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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