Conformational activation of talin by RIAM triggers integrin-mediated cell adhesion

Jun Yang, Liang Zhu, Hao Zhang, Jamila Hirbawi, Koichi Fukuda, Pallavi Dwivedi, Jianmin Liu, Tatiana Byzova, Edward F. Plow, Jinhua Wu () and Jun Qin ()
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Jun Yang: Lerner Research Institute, Cleveland Clinic
Liang Zhu: Lerner Research Institute, Cleveland Clinic
Hao Zhang: Developmental Therapeutics Program, Fox Chase Cancer Center
Jamila Hirbawi: Lerner Research Institute, Cleveland Clinic
Koichi Fukuda: Lerner Research Institute, Cleveland Clinic
Pallavi Dwivedi: Lerner Research Institute, Cleveland Clinic
Jianmin Liu: Lerner Research Institute, Cleveland Clinic
Tatiana Byzova: Lerner Research Institute, Cleveland Clinic
Edward F. Plow: Lerner Research Institute, Cleveland Clinic
Jinhua Wu: Developmental Therapeutics Program, Fox Chase Cancer Center
Jun Qin: Lerner Research Institute, Cleveland Clinic

Nature Communications, 2014, vol. 5, issue 1, 1-9

Abstract: Abstract The membrane localization and activation of cytoskeletal protein talin are key steps to initiate the integrin transmembrane receptors’ activation, which mediates many cellular adhesive responses such as cell migration, spreading and proliferation. RIAM, a membrane anchor and small GTPase RAP1 effector, is known to bind to the C-terminal rod domain of talin (talin-R) and promote localizations of talin to the membrane. Through systematic mapping analysis, we find that RIAM also binds to the N-terminal head of talin (talin-H), a crucial domain involved in binding and activating integrins. We show that the RIAM binding to talin-H sterically occludes the binding of a talin-R domain that otherwise masks the integrin-binding site on talin-H. We further provide functional evidence that such RIAM-mediated steric unmasking of talin triggers integrin activation. Our findings thus uncover a novel role for RIAM in conformational regulation of talin during integrin activation and cell adhesion.

Date: 2014
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DOI: 10.1038/ncomms6880

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