Access Restriction

Author Krzysztof Palczewski§i.
Source CiteSeerX
Content type Text
File Format PDF
Subject Domain (in DDC) Computer science, information & general works ♦ Data processing & computer science
Subject Keyword Rod Outer Segment ♦ Endogenous Protein Kinase ♦ Gtpase-accelerating Protein ♦ Visual Protein Transducin ♦ Rgs9-1 Phos-phorylation ♦ Recombinant Rgs9-1 ♦ Dur-ing Recovery ♦ Phosphate Mol ♦ S475a Mutant ♦ Synthetic Peptide ♦ Rgs9-1 Kinase ♦ Average Stoichiometry ♦ Rod Outer Seg-ment Membrane ♦ Endogenous Kinase ♦ Similar Peptide ♦ Dark-adapted Bovine Rod Outer Segment ♦ S475a Substitution ♦ Robust Phosphorylation ♦ Ubiquitous Rg Protein Family ♦ Single Major Site ♦ Rgs9-1 Phosphorylation ♦ Mass Spectrometry ♦ G-32p Atp
Abstract Inactivation of the visual G protein transducin, dur-ing recovery from photoexcitation, is regulated by RGS9-1, a GTPase-accelerating protein of the ubiquitous RGS protein family. Incubation of dark-adapted bovine rod outer segments with [g-32P]ATP led to RGS9-1 phos-phorylation by an endogenous kinase in rod outer seg-ment membranes, with an average stoichiometry of 0.2– 0.45 mol of phosphates/mol of RGS9-1. Mass spectrometry revealed a single major site of phosphoryl-ation, Ser475. The kinase responsible catalyzed robust phosphorylation of recombinant RGS9-1 and not of an S475A mutant. A synthetic peptide corresponding to the region surrounding Ser475 was also phosphorylated, and a similar peptide with the S475A substitution inhibited RGS9-1 phosphorylation. The RGS9-1 kinase is a periph-
Educational Role Student ♦ Teacher
Age Range above 22 year
Educational Use Research
Education Level UG and PG ♦ Career/Technical Study
Publisher Date 2001-01-01