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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

The pleckstrin homology domain of phospholipase C-beta2 as an effector site for Rac.

Increasing evidence links the activation of Rho family GTPases to the stimulation of lipid hydrolysis catalyzed by phospholipase C (PLC)-beta isozymes. To better define this relationship, members of a library of recombinant Rho GTPases were screened for their capacity to directly engage various purified PLC-beta isozymes. Of the 17 tested members of the Rho family, only the active isoforms of Rac (Rac1, Rac2, and Rac3) both stimulate PLC-beta activity in vivo and bind PLC-beta2 and PLC-beta3, but not PLC-beta1, in vitro. Furthermore, the recognition site for Rac GTPases was localized to the pleckstrin homology (PH) domain of PLC-beta2, and this PH domain is fully sufficient to selectively interact with the active versions of the Rac GTPases, but not with other similar Rho GTPases. Together, these findings present a quantitative evaluation of the direct interactions between Rac GTPases and PLC-beta isozymes and define a novel role for the PH domain of PLC-beta2 as a putative effector site for Rac GTPases.[1]


  1. The pleckstrin homology domain of phospholipase C-beta2 as an effector site for Rac. Snyder, J.T., Singer, A.U., Wing, M.R., Harden, T.K., Sondek, J. J. Biol. Chem. (2003) [Pubmed]
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