Analyses of Rem/RGK signaling and biological activity.
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 beta-subunits and describe electrophysiological analyses for characterizing Rem-mediated regulation of L-type Ca2+ channel activity.
Andres
Douglas A
DA
Department of Molecular and Cellular Biochemistry, University of Kentucky College of Medicine, Lexington, Kentucky, USA.
Crump
Shawn M
SM
Correll
Robert N
RN
Satin
Jonathan
J
Finlin
Brian S
BS
D000818:Animals; D020746:Calcium Channels, L-Type / Q000502:physiology; D002478:Cells, Cultured; D006224:Cricetinae; D004594:Electrophysiology; D006801:Humans; D047468:Immunoprecipitation; D051379:Mice; D020559:Monomeric GTP-Binding Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D011485:Protein Binding; D014162:Transfection
D020746:Calcium Channels, L-Type; C108135:Rem protein, mouse; D020559:Monomeric GTP-Binding Proteins