The PH domain: a common piece in the structural pathcwork of signalling proteins

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Abstract

The ‘pleckstrin homology’ domain is an approximately 100-residue protein module that has recently been added to the domain catalogue of signalling proteins. For this review we have made an extensive database search using a profile search method, and found a number of additional proteins that may contain PH domains. The PH domain is present in many kinases, isoforms of phospholipase C, GTPases, GTPase-activating proteins and nucleotide-exchange factors, including such proteins as Vav, Dbl and Bcr, and there are two PH domains in a guanine-nucleotide releasing factor of Ras. Many PH-domain-containing proteins interact with GTP-binding proteins. We have also identified a PH domain in β-adrenergic receptor kinase exactly in the region that has already been shown to be involved in binding to the β and γ subunits of a heterotrimeric G protein. This suggests that PH domains may be involved in interactions with GTP-binding proteins.

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      gk216 is a 1381 bp deletion followed by 56 out of frame amino acids before resulting in a stop near the beginning of the DH homology domain (Lin et al., 2012). This allele also eliminates the following PH domain, both of which are required for GEF activity (Musacchio et al., 1993; Rossman and Sondek, 2005). Thus because gk216 lacks GEF activity, this represents a null allele (we show below that gk216 lacks protein by immunostaining).

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