Calmodulin binding to the small GTPase Ral requires isoprenylated Ral.

@article{Sidhu2005CalmodulinBT,
  title={Calmodulin binding to the small GTPase Ral requires isoprenylated Ral.},
  author={Ranjinder S Sidhu and Sherif M Elsaraj and Ognjen Grujic and Rajinder Pal Bhullar},
  journal={Biochemical and biophysical research communications},
  year={2005},
  volume={336 1},
  pages={105-9}
}
Ral, a member of the Ras-p21 superfamily of small GTPases, has been shown to require the calcium-signaling protein calmodulin (CaM) for activation. In the present work, we investigated the properties of the Ral-CaM interaction. Using CaM affinity binding assay with lysates from mammalian cells overexpressing various Ral mutants, we found that RalB(V23, DeltaCAAX) lacking the C-terminal isoprenylation region bound significantly less efficiently to CaM. Binding of other mutants containing… CONTINUE READING