Structure of the Sec14 domain of Kalirin reveals a distinct class of lipid-binding module in RhoGEFs

Yunfeng Li; Yulia Pustovalova; Tzanko I. Doukov; Jeffrey C. Hoch; Richard E. Mains; Betty A. Eipper; Bing Hao

doi:10.1038/s41467-022-35678-4

Nature Communications (Jan 2023)

Structure of the Sec14 domain of Kalirin reveals a distinct class of lipid-binding module in RhoGEFs

Yunfeng Li,
Yulia Pustovalova,
Tzanko I. Doukov,
Jeffrey C. Hoch,
Richard E. Mains,
Betty A. Eipper,
Bing Hao

Affiliations

Yunfeng Li: Department of Molecular Biology and Biophysics, University of Connecticut Health Center
Yulia Pustovalova: Department of Molecular Biology and Biophysics, University of Connecticut Health Center
Tzanko I. Doukov: Macromolecular Crystallography Group, Stanford Synchrotron Radiation Light Source, SLAC National Accelerator Laboratory, Stanford University
Jeffrey C. Hoch: Department of Molecular Biology and Biophysics, University of Connecticut Health Center
Richard E. Mains: Department of Neuroscience, University of Connecticut Health Center
Betty A. Eipper: Department of Molecular Biology and Biophysics, University of Connecticut Health Center
Bing Hao: Department of Molecular Biology and Biophysics, University of Connecticut Health Center

DOI: https://doi.org/10.1038/s41467-022-35678-4
Journal volume & issue: Vol. 14, no. 1
pp. 1 – 14

Abstract

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A subset of Sec14 domain proteins use their gated hydrophobic pocket to bind and transport lipids. Here the authors provide structural and biochemical data revealing how the Sec14-fold of a Rho-GEF forms a surface groove that interacts with lysolipids.

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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