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    Nat Struct Mol Biol. 2006 Dec;13(12):1135-40. Epub 2006 Nov 19.

    Crystal structure of Rac1 bound to its effector phospholipase C-beta2.

    Jezyk MR, Snyder JT, Gershberg S, Worthylake DK, Harden TK, Sondek J.

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    Department of Biochemistry and Biophysics The University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599, USA.

    Abstract

    Although diverse signaling cascades require the coordinated regulation of heterotrimeric G proteins and small GTPases, these connections remain poorly understood. We present the crystal structure of the GTPase Rac1 bound to phospholipase C-beta2 (PLC-beta2), a classic effector of heterotrimeric G proteins. Rac1 engages the pleckstrin-homology (PH) domain of PLC-beta2 to optimize its orientation for substrate membranes. Gbetagamma also engages the PH domain to activate PLC-beta2, and these two activation events are compatible, leading to additive stimulation of phospholipase activity. In contrast to PLC-delta, the PH domain of PLC-beta2 cannot bind phosphoinositides, eliminating this mode of regulation. The structure of the Rac1-PLC-beta2 complex reveals determinants that dictate selectivity of PLC-beta isozymes for Rac GTPases over other Rho-family GTPases, and substitutions within PLC-beta2 abrogate its stimulation by Rac1 but not by Gbetagamma, allowing for functional dissection of this integral signaling node.

    PMID:
    17115053
    [PubMed - indexed for MEDLINE]

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