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

38Citations
Citations of this article
12Readers
Mendeley users who have this article in their library.

Abstract

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.

Cite

CITATION STYLE

APA

Abu-Elneel, K., Karchi, M., & Ravid, S. (1996). Dictyostelium myosin II is regulated during chemotaxis by a novel protein kinase C. Journal of Biological Chemistry, 271(2), 977–984. https://doi.org/10.1074/jbc.271.2.977

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free