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Journal Article

Alternative splicing of Rac1 generates Rac1b, a self-activating GTPase.

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Blumenstein,  Lars
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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http://www.jbc.org/content/279/6/4743.full.pdf
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https://doi.org/10.1074/jbc.M310281200
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Citation

Fiegen, D., Haeusler, L., Blumenstein, L., Herbrand, U., Dvorsky, R., Vetter, I. R., et al. (2004). Alternative splicing of Rac1 generates Rac1b, a self-activating GTPase. The Journal of Biological Chemistry, 279(6), 4743-4749. doi:10.1074/jbc.M310281200.


Cite as: https://hdl.handle.net/21.11116/0000-0001-EE27-8
Abstract
Rac1b was recently identified in malignant colorectal tumors as an alternative splice variant of Rac1 containing a 19-amino acid insertion next to the switch II region. The structures of Rac1b in the GDP- and the GppNHp-bound forms, determined at a resolution of 1.75 A, reveal that the insertion induces an open switch I conformation and a highly mobile switch II. As a consequence, Rac1b has an accelerated GEF-independent GDP/GTP exchange and an impaired GTP hydrolysis, which is restored partially by GTPase-activating proteins. Interestingly, Rac1b is able to bind the GTPase-binding domain of PAK but not full-length PAK in a GTP-dependent manner, suggesting that the insertion does not completely abolish effector interaction. The presented study provides insights into the structural and biochemical mechanism of a self-activating GTPase.