Phosphorylated and non-phosphorylated connexin-32 molecules in gap junction plaques are protected against calpain proteolysis after phosphorylation by protein kinase C

1994 ◽  
Vol 22 (3) ◽  
pp. 793-796 ◽  
Author(s):  
Maribel Elvira ◽  
Kevin K. W. Wang ◽  
Antonio Villalobo
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Gap Junction ◽  
Connexin 32 ◽  
Kinase C

scholarly journals Phosphorylation of connexin-32 by protein kinase C prevents its proteolysis by mu-calpain and m-calpain

1993 ◽  
Vol 268 (19) ◽  
pp. 14294-14300
Author(s):  
M. Elvira ◽  
J.A. Díez ◽  
K.K. Wang ◽  
A. Villalobo
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Connexin 32 ◽  
Kinase C

Spatio-Temporal Dissection of Protein Kinase C-Mediated Phosphorylation of the Gap Junction Protein Connexin43

2012 ◽  
Vol 18 (S2) ◽  
pp. 144-145
Author(s):  
A.C. Cone ◽  
A. Wu-Zhang ◽  
A.C. Newton ◽  
G.E. Sosinsky
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Gap Junction ◽  
Kinase C ◽  
Junction Protein ◽  
Gap Junction Protein ◽  
Spatio Temporal

Extended abstract of a paper presented at Microscopy and Microanalysis 2012 in Phoenix, Arizona, USA, July 29 – August 2, 2012.

Phosphorylation of liver gap junction protein by protein kinase C

FEBS Letters ◽  
1987 ◽  
Vol 210 (2) ◽  
pp. 169-172 ◽  
Author(s):  
Akira Takeda ◽  
Eikichi Hashimoto ◽  
Hirohei Yamamura ◽  
Takashi Shimazu
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Gap Junction ◽  
Kinase C ◽  
Junction Protein ◽  
Gap Junction Protein

Mechanism of regulation of the gap junction protein connexin 43 by protein kinase C-mediated phosphorylation

2004 ◽  
Vol 286 (3) ◽  
pp. C647-C654 ◽  
Author(s):  
Xiaoyong Bao ◽  
Guillermo A. Altenberg ◽  
Luis Reuss
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Gap Junction ◽  
Connexin 43 ◽  
Molecular Mechanisms ◽  
Xenopus Laevis Oocytes ◽  
Solute Permeability ◽  
Kinase C ◽  
Junction Protein ◽  
Gap Junction Protein

Phosphorylation of the gap junction protein connexin 43 (Cx43) by protein kinase C (PKC) decreases dye coupling in many cell types. We report an investigation of the regulation by PKC of Cx43 gap junctional hemichannels (GJH) expressed in Xenopus laevis oocytes. The activity of GJH was assessed from the uptake of hydrophilic fluorescent probes. PKC inhibitors increased probe uptake in isolated oocytes expressing recombinant Cx43, indicating that the regulatory effect occurs at the hemichannel level. We identified by mutational analysis the carboxy-terminal (CT) domain sequences involved in this response. We found that 1) Ser368 is responsible for the regulation of Cx43 GJH solute permeability by PKC-mediated phosphorylation, 2) CT domain residues 253-270 and 288-359 are not necessary for the effect of PKC, and 3) the prolinerich CT region is not involved in the effect of phosphorylation by PKC. Our results demonstrate that Ser368 (but not Ser372) is involved in the regulation of Cx43 solute permeability by PKC-mediated phosphorylation, and we conclude that different molecular mechanisms underlie the regulation of Cx43 by intracellular pH and PKC-mediated phosphorylation.

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