Tyrosine phosphorylation of connexin 43 by v-Src is mediated by SH2 and SH3 domain interactions.

@article{Kanemitsu1997TyrosinePO,
  title={Tyrosine phosphorylation of connexin 43 by v-Src is mediated by SH2 and SH3 domain interactions.},
  author={Martha Y. Kanemitsu and Lenora W. M. Loo and St{\'e}phanie Simon and Alan F. Lau and Walter Eckhart},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 36},
  pages={22824-31}
}
Reduction of gap junctional communication in v-src transformed cells is accompanied by tyrosine phosphorylation of the gap junction protein, connexin 43 (Cx43). Cx43 is phosphorylated on tyrosine by v-Src. The Src homology 3 (SH3) and Src homology 2 (SH2) domains of v-Src mediate interactions with substrate proteins. SH3 domains interact with proline-rich peptide motifs. SH2 domains associate with short amino acid sequences containing phosphotyrosine. We present evidence that the SH3 and SH2… CONTINUE READING

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The connexin 43 C-terminus: A tail of many tales.

Biochimica et biophysica acta. Biomembranes • 2018

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