Phosphorylation of critical serine residues in Gem separates cytoskeletal reorganization from down-regulation of calcium channel activity.

@article{Ward2004PhosphorylationOC,
  title={Phosphorylation of critical serine residues in Gem separates cytoskeletal reorganization from down-regulation of calcium channel activity.},
  author={Yvona Ward and Beth Spinelli and Michael J. Quon and Huifen Chen and Stephen R Ikeda and Kathleen Kelly},
  journal={Molecular and cellular biology},
  year={2004},
  volume={24 2},
  pages={
          651-61
        }
}
Gem is a small GTP-binding protein that has a ras-like core and extended chains at each terminus. The primary structure of Gem and other RGK family members (Rad, Rem, and Rem2) predicts a GTPase deficiency, leading to the question of how Gem functional activity is regulated. Two functions for Gem have been demonstrated, including inhibition of voltage-gated calcium channel activity and inhibition of Rho kinase-mediated cytoskeletal reorganization, such as stress fiber formation and neurite… CONTINUE READING
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