Phosphorylation of the postsynaptic density glycoprotein gp180 by endogenous tyrosine kinase.

Incubation of postsynaptic densities (PSDs) with [gamma-32P]adenosine triphosphate (ATP) results in the phosphorylation of a number of proteins. Of these, phosphoproteins with apparent molecular weights (Mr) of 51,000, 180,000, 300,000, 320,000 and 370,000 contain 32P which is resistant to digestion with hot KOH suggesting the presence of [32P]phosphotyrosine residues. Phosphoamino acid analysis of total 32P-labelled PSDs identified [32P]phosphotyrosine as well as phosphoserine and phosphothreonine as products of the phosphorylation reaction. The PSD-specific glycoprotein gp180 was isolated from 32P-labelled PSDs and shown to contain [32P]phosphotyrosine. The results identify tyrosine kinase as a component of purified PSDs and gp180 as an endogenous substrate for this enzyme.