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62 lck ligand (zeta-interacting protein (ZIP)) is a cytoplasmic protein that binds to the SH2 domain of lck (a T cell src tyrosine kinase) in the absence of a phosphotyrosine in either protein. The ubiquitously expressed p62 lck ligand contains a cysteine rich region that is similar to a zinc finger domain, a G protein binding region, a PEST sequence, and several phosphorylation sites. Deletion of the p62 lck ligand N-terminal domain has been reported to abrogate its binding to lck. However, mutation of the tyrosine did not have an effect. In addition, p62 lck ligand binds to the pseudosubstrate region of the PKCζ catalytic domain. In turn, PKCζ phosphorylates p62. p62 lck ligand binds to the dimerization region of PKCζ, thereby inhibiting PKCζ-PKCζ interaction. This suggests that p62 lck ligand may compete with PKCζ. However, it requires PKCζ for proper subcellular localization. These data suggest that p62 lck ligand may be part of the protein bridge that links PKCζ to the tyrosine kinases involved in signaling pathways.Immunofluorescence, Immunoprecipitation, Western Blotting
