Rem (Rad and Gem related) is a member of the RGK family of Ras-related GTPases that also includes Rad, Rem2, and Gem/Kir. All RGK proteins share structural features that are distinct from other Ras-related proteins, including several nonconservative amino acid substitutions within regions known to participate in nucleotide binding and hydrolysis and a C-terminal extension that contains regulatory sites that seem to control both subcellular location and function. Rem is known to modulate two distinct signal transduction pathways, regulating both cytoskeletal reorganization and voltage-gated Ca2+ channel activity. In this chapter, we summarize the experimental approaches used to characterize the interaction of Rem with 14-3-3 proteins and Ca2+ channel β-subunits and describe electrophysiological analyses for characterizing Rem-mediated regulation of L-type Ca2+ channel activity.
|Number of pages||15|
|Journal||Methods in Enzymology|
|State||Published - 2006|
Bibliographical noteFunding Information:
We acknowledge W. Peavler for his contributions to these studies. This work was supported in part by United States Public Health Service Grants HL‐072936 (D. A. A.) and HL‐074091 (J. S.), National Institutes of Health Grant P20RR0171 from the COBRE program of the NCRR (to D. A. A.), and by a Predoctoral Fellowship from the American Heart Association, Ohio Valley Affiliate (to R. N. C). J. S. is an Established Investigator of the American Heart Association.
ASJC Scopus subject areas
- Molecular Biology