Dictyostelium myosin II is regulated during chemotaxis by a novel protein kinase C.

The myosin II heavy chain (MHC)-specific protein kinase C isolated from Dictyostelium discoideum has been implicated in the regulation of myosin II assembly in response to the chemoattractant, cAMP (Ravid, S., and Spudich, J. A. (1989) J. Biol. Chem. 264, 15144-15150). Here we report that elimination of results in the abolishment of MHC phosphorylation in response to cAMP. Cells devoid of MHC-duanyu1531 exhibit substantial myosin II overassembly, as well as aberrant cell polarization, chemotaxis, and morphological differentiation. Cells overexpressing the MHC-duanyu1531 contain highly phosphorylated MHC and exhibit impaired myosin II localization and no apparent cell polarization and chemotaxis. The results presented here provide direct evidence that MHC-duanyu1531 phosphorylates MHC in response to cAMP and plays an important role in the regulation of myosin II localization during chemotaxis.

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