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Several laboratories have demonstrated a decrease in gap
junctional communication in cells transformed by the src oncogene of the Rous sarcoma virus. The decrease in gap junctional
communication was associated with tyrosine phosphorylation of the gap
junction protein, connexin 43 (Cx43). This study was initiated to
determine if the phosphorylation of Cx43 is the result of a direct
kinase-substrate interaction between the highly active tyrosine kinase,
pp60
Volume 270,
Number 21,
Issue of May 26, pp. 12751-12761, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
-mediated
Phosphorylation of Connexin 43, a Gap Junction Protein
, and Cx43. Previous
biochemical studies have been limited by the low levels of Cx43 protein
in fibroblast cell lines. To obtain larger quantities of Cx43, we
constructed a recombinant baculovirus expressing Cx43 in Spodoptera
frugiperda (Sf-9) cells and subsequently purified the expressed
Cx43 by immunoaffinity chromatography. We observed that this partially
purified Cx43 was phosphorylated on tyrosine in vitro in the
presence of kinase-active pp60
. Phosphotryptic
peptide mapping indicated that the in vitro phosphorylated
Cx43 contained phosphopeptides which comigrated with a subset of
tryptic peptides prepared from Cx43 phosphorylated in vivo.
Furthermore, coinfection of Sf-9 cells with recombinant baculoviruses
encoding pp60
and Cx43 resulted in
the accumulation of phosphotyrosine in Cx43. Taken together, the
evidence presented in this paper demonstrates that kinase active
pp60
is capable of phosphorylating
Cx43 in a direct manner. Since the presence of phosphotyrosine on Cx43
is correlated with the down-regulation of gap-junctional communication,
these results suggest that pp60
regulates gap junctional gating activity via tyrosine
phosphorylation of Cx43.
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