Chemoattractant-mediated increases in cGMP induce changes in Dictyostelium myosin II heavy chain-specific protein kinase C activities.
Open Access
- 15 August 1996
- journal article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 134 (4), 911-921
- https://doi.org/10.1083/jcb.134.4.911
Abstract
Myosin II heavy chain (MHC)-specific protein kinase C (MHC-PKC) isolated from the ameba, Dictyostelium discoideum, regulates myosin II assembly and localization in response to the chemoattractant cAMP (Abu-Elneel et al. 1996. J. Biol. Chem. 271:977- 984). Recent studies have indicated that cAMP-induced cGMP accumulation plays a role in the regulation of myosin II phosphorylation and localization (Liu, G., and P. Newell. 1991. J. Cell. Sci. 98: 483-490). This report describes the roles of cAMP and cGMP in the regulation of MHC-PKC membrane association, phosphorylation, and activity (hereafter termed MHC-PKC activities). cAMP stimulation of Dictyostelium cells resulted in translocation of MHC-PKC from the cytosol to the membrane fraction, as well as increasing in MHC-PKC phosphorylation and in its kinase activity. We present evidence that MHC is phosphorylated by MHC-PKC in the cell cortex which leads to myosin II dissociation from the cytoskeleton. Use of Dictyostelium mutants that exhibit aberrant cAMP-induced increases in cGMP accumulation revealed that MHC-PKC activities are regulated by cGMP. Dictyostelium streamer F mutant (stmF), which produces a prolonged peak of cGMP accumulation upon cAMP stimulation, exhibits prolonged increases in MHC-PKC activities. In contrast, Dictyostelium KI-10 mutant that lacks the normal cAMP-induced cGMP response, or KI-4 mutant that shows nearly normal cAMP-induced cGMP response but has aberrant cGMP binding activity, show no changes in MHC-PKC activities. We provide evidence that cGMP may affect MHC-PKC activities via the activation of cGMP-dependent protein kinase which, in turn, phosphorylates MHC-PKC. The results presented here indicate that cAMP-induced cGMP accumulation regulates myosin II phosphorylation and localization via the regulation of MHC-PKC.Keywords
This publication has 42 references indexed in Scilit:
- Dictyostelium Myosin II Is Regulated during Chemotaxis by a Novel Protein Kinase CJournal of Biological Chemistry, 1996
- Aberrant cGMP-binding activity in non-chemotactic Dictyostelium discoideum mutantsBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1995
- CONTROL OF NONMUSCLE MYOSINS BY PHOSPHORYLATIONAnnual Review of Biochemistry, 1992
- Quantification of motility and area changes ofDictyostelium discoideum amoebae in response to chemoattractantsJournal of Muscle Research and Cell Motility, 1988
- Transient increase of the intracellular Ca2+ concentration during chemotactic signal transduction in Dictyostelium discoideum cellsDifferentiation, 1988
- Relationship of pseudopod extension to chemotactic hormone‐induced actin polymerization in amoeboid cellsJournal of Cellular Biochemistry, 1988
- K-252 compounds, novel and potent inhibitors of protein kinase C and cyclic nucleotide-dependent protein kinasesBiochemical and Biophysical Research Communications, 1986
- Altered cGMP‐phosphodiesterase activity in chemotactic mutants of Dictyostelium discoideumFEBS Letters, 1982
- Cyclic AMP and folic acid mediated cyclic GMP accumulation in Dictyostelium discoideumFEBS Letters, 1977
- Cyclic GMP in Dictyostelium discoideum Oscillations and pulses in response to folic acid and cyclic AMP signalsFEBS Letters, 1977