scholarly journals Autophosphorylation ofDictyosteliumMyosin II Heavy Chain-specific Protein Kinase C Is Required for Its Activation and Membrane Dissociation

1997 ◽  
Vol 272 (2) ◽  
pp. 828-834 ◽  
Author(s):  
Adi Dembinsky ◽  
Hila Rubin ◽  
Shoshana Ravid
1996 ◽  
Vol 134 (4) ◽  
pp. 911-921 ◽  
Author(s):  
A Dembinsky ◽  
H Rubin ◽  
S Ravid

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.


1990 ◽  
Vol 10 (12) ◽  
pp. 3782-3792 ◽  
Author(s):  
A Represa ◽  
JC Deloulme ◽  
M Sensenbrenner ◽  
Y Ben-Ari ◽  
J Baudier

1995 ◽  
Vol 270 (17) ◽  
pp. 10314-10322 ◽  
Author(s):  
Takayuki Sato ◽  
Dian-Mo Xiao ◽  
Hua Li ◽  
Freesia L. Huang ◽  
Kuo-Ping Huang

FEBS Letters ◽  
1988 ◽  
Vol 231 (1) ◽  
pp. 221-224 ◽  
Author(s):  
Yoshinori Asaoka ◽  
Ushio Kikkawa ◽  
Kazuo Sekiguchi ◽  
Mark S. Shearman ◽  
Yoshiyuki Kosaka ◽  
...  

2021 ◽  
Vol 11 (3) ◽  
pp. 744-759
Author(s):  
Rong Xiao ◽  
Hai-Chun Zhao ◽  
Tian-Tian Yan ◽  
Qiong Zhang ◽  
Yue-Sheng Huang

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