Phosphorylation of Gz in human platelets. Selectivity and site of modification.
作者： K.M. Lounsbury , P.J. Casey , L.F. Brass , D.R. Manning
DOI: 10.1016/S0021-9258(18)54743-8
关键词:
摘要: Abstract We have demonstrated previously that the G protein alpha subunit Gz (or Gx alpha) in human platelets is subject to phosphorylation by agents activate kinase C, including phorbol 12-myristate 13-acetate, thrombin, and thromboxane A2 analog U46619. examine here site selectivity of both vitro using recombinant subunits situ permeabilized intact platelets. Protein C catalyzes rapid nearly stoichiometric alpha, with modification occurring preferentially for GDP-bound form subunit. Under same conditions, Gi 1, 2, 3, Gs alpha-S, alpha-L, Go 1 was minimal. Phosphorylation rGz platelet occurs at a serine residue near amino terminus. This conclusion supported phosphoamino acid analysis incorporation radiolabel from [gamma-32P]ATP into amino-terminal CNBr peptide (residues 2-53 encoded protein). One antisera used this study (6354, directed toward residues 24-33) recognizes only nonphosphorylated providing strong evidence Ser25 or Ser27 phosphorylation. Results obtained 6354 also suggest ester-promoted approaches mol phosphate per
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