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

Kawther Abu-Elneel, Miri Karchi, Shoshana Ravid*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

38 Scopus citations


The myosin II heavy chain (MHC)-specific protein kinase C (MHC-PKC) 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 MHC-PKC results in the abolishment of MHC phosphorylation in response to cAMP. Cells devoid of MHC-PKC exhibit substantial myosin II overassembly, as well as aberrant cell polarization, chemotaxis, and morphological differentiation. Cells overexpressing the MHC-PKC 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-PKC phosphorylates MHC in response to cAMP and plays an important role in the regulation of myosin II localization during chemotaxis.

Original languageAmerican English
Pages (from-to)977-984
Number of pages8
JournalJournal of Biological Chemistry
Issue number2
StatePublished - 12 Jan 1996


Dive into the research topics of 'Dictyostelium myosin II is regulated during chemotaxis by a novel protein kinase C'. Together they form a unique fingerprint.

Cite this