Structure of Rap1b bound to talin reveals a pathway for triggering integrin activation

Liang Zhu; Jun Yang; Thomas Bromberger; Ashley Holly; Fan Lu; Huan Liu; Kevin Sun; Sarah Klapproth; Jamila Hirbawi; Tatiana V. Byzova; Edward F. Plow; Markus Moser; Jun Qin

doi:10.1038/s41467-017-01822-8

Nature Communications (Nov 2017)

Structure of Rap1b bound to talin reveals a pathway for triggering integrin activation

Liang Zhu,
Jun Yang,
Thomas Bromberger,
Ashley Holly,
Fan Lu,
Huan Liu,
Kevin Sun,
Sarah Klapproth,
Jamila Hirbawi,
Tatiana V. Byzova,
Edward F. Plow,
Markus Moser,
Jun Qin

Affiliations

Liang Zhu: Department of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic
Jun Yang: Department of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic
Thomas Bromberger: Max-Planck-Institute of Biochemistry, Department of Molecular Medicine
Ashley Holly: Department of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic
Fan Lu: Department of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic
Huan Liu: Department of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic
Kevin Sun: Department of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic
Sarah Klapproth: Max-Planck-Institute of Biochemistry, Department of Molecular Medicine
Jamila Hirbawi: Department of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic
Tatiana V. Byzova: Department of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic
Edward F. Plow: Department of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic
Markus Moser: Max-Planck-Institute of Biochemistry, Department of Molecular Medicine
Jun Qin: Department of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic

DOI: https://doi.org/10.1038/s41467-017-01822-8
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 12

Abstract

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The transmembrane receptor integrin is activated by talin, but so far it has remained elusive how talin is recruited to the plasma membrane. Here, the authors identify the Rap1-mediated membrane-targeting mechanism for talin, present the Rap1b/talin-F0 structure and show that talin is a direct Rap1b effector.

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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