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Stimulation of B cells by clustering their surface immunoglobulins (sIg) leads to enhanced phosphorylation of several cellular proteins on Ser and Tyr residues. The type II Fc gamma receptor (Fc gamma RII) is one of those proteins that undergo Ser phosphorylation. Upon affinity isolation of the Fc gamma RII, several molecular entities are coisolated from Triton X-100 lysates of BL41 Burkitt lymphoma line which undergo "in vitro" (cell free) phosphorylation in the immune complex-associated kinase assay. Furthermore, several molecules phosphorylated on Tyr upon sIgM cross-linking in the intact cells are coisolated with Fc gamma RII. The 59-kDa coprecipitated component is identified as the protein-tyrosine kinase (PTK) fyn. Clustering the sIgM molecules enhanced the in vitro phosphorylation of all molecules coprecipitated with Fc gamma RII as well as that of the exogenously added PTK substrate, enolase. Kinase renaturation assays suggest that at least two major renaturable protein kinases (59 kDa and 85-90 kDa) associate with Fc gamma RII. Whereas the 59-kDa component comigrates with the PTK fyn, the 85- to 90-kDa one is an unidentified Ser/Thr kinase. These data suggest that Fc gamma RII exists in the B-cell membrane as part of a multimolecular complex including protein kinases, activities of which are regulated by clustering of the antigen receptors.

Protein-tyrosine kinase activity tightly associated with human type II Fc gamma receptors.