Amino acid residue Val362 plays a critical role in maintaining the structure of C terminus of connexin 50 and in lens epithelial-fiber differentiation.

@article{Liu2010AminoAR,
  title={Amino acid residue Val362 plays a critical role in maintaining the structure of C terminus of connexin 50 and in lens epithelial-fiber differentiation.},
  author={Xiaoping Liu and Eric A Banks and Xun Sean Yu and Sumin Gu and Janelle L. Lauer and Gregg B Fields and Jean X Jiang},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 24},
  pages={18415-22}
}
We have previously shown that connexin (Cx) 50, unlike the other two lens connexins, Cx43 and Cx46, promotes chicken lens epithelial-fiber differentiation in a channel-independent manner. Here, we show that deletion of the PEST motif at the C terminus (CT) domain of Cx50 attenuates the stimulatory effect of Cx50 on lens fiber differentiation. Valine 362, a… CONTINUE READING