Novel domains in NADPH oxidase subunits, sorting nexins, and PtdIns 3‐kinases: binding partners of SH3 domains?

CP Ponting - Protein Science, 1996 - Wiley Online Library
Protein Science, 1996Wiley Online Library
Two SH3 domain‐containing cytosolic components of the NADPH oxidase, p47phox and
p40phox, are shown by analyses of their sequences to contain single copies of a novel class
of domain, the PX (phox) domain. Homologous domains are demonstrated to be present in
the Cpk class of phosphatidylinositol 3‐kinase, S. cerevisiae Bem1p, and S. pombe Scd2,
and a large family of human sorting nexin 1 (SNX1) homologues. The majority of these
domains contains a polyproline motif, typical of SH3 domain‐binding proteins. Two further …
Abstract
Two SH3 domain‐containing cytosolic components of the NADPH oxidase, p47phox and p40phox, are shown by analyses of their sequences to contain single copies of a novel class of domain, the PX (phox) domain. Homologous domains are demonstrated to be present in the Cpk class of phosphatidylinositol 3‐kinase, S. cerevisiae Bem1p, and S. pombe Scd2, and a large family of human sorting nexin 1 (SNX1) homologues. The majority of these domains contains a polyproline motif, typical of SH3 domain‐binding proteins. Two further findings are reported. A third NADPH oxidase subunit, p67phox, is shown to contain four tetratricopeptide repeats (TPRs) within its N‐terminal RaclGTP‐binding region, and a 28 residue motif in p40phox is demonstrated to be present in protein kinase C isoforms τ/λ and ζ, and in three ZZ domain‐containing proteins.
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