Mechanism of IRSp53 inhibition by 14-3-3

David J. Kast; Roberto Dominguez

doi:10.1038/s41467-019-08317-8

Nature Communications (Jan 2019)

Mechanism of IRSp53 inhibition by 14-3-3

David J. Kast,
Roberto Dominguez

Affiliations

David J. Kast: Department of Physiology, Perelman School of Medicine, University of Pennsylvania
Roberto Dominguez: Department of Physiology, Perelman School of Medicine, University of Pennsylvania

DOI: https://doi.org/10.1038/s41467-019-08317-8
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 14

Abstract

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IRSp53 is a key regulator of filopodia formation and cell migration. Here, the authors elucidate a mechanism of phosphorylation-dependent inhibition of IRSp53 by 14-3-3, which impedes the interactions of IRSp53 with membranes and downstream cytoskeletal effectors.

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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