β2-Chimaerin is a novel target for diacylglycerol: Binding properties and changes in subcellular Localization mediated by ligand binding To its C1 domain

摘要

The members of the chimaerin family of Rac-GTPase-activating proteins possess a single C1 domain with high homology to those present in protein kinase C(PKC) isozymes. This domain in PCKs is involved in phorbol ester and diacylglycerol (DAG) bindign. We previously have demosntrated that one of the chimaerin isforms, β2-chimarin, binds phorbol esters with high affinity. In this study we analyzed the properties of β2-chimaerin as a DAG receptor by using a series of conformationally constrained cyclic DAG ana- logues (DAG lactones) as probles.