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Voltage-dependent calcium (Ca2+) channels are involved in many specialized cellular functions and are controlled by a diversity of intracellular signals. Recently, members of the RGK family of small GTPases (Rem, Rem2, Rad, Gem/Kir) have been identified as novel contributors to the regulation of L-type calcium channel activity. In this study, microarray(More)
Cardiac voltage-gated L-type Ca channels (Ca(V)) are multiprotein complexes, including accessory subunits such as Ca(V)beta2 that increase current expression. Recently, members of the Rad and Gem/Kir-related family of small GTPases have been shown to decrease current, although the mechanism remains poorly defined. In this study, we evaluated the(More)
The Rem, Rem2, Rad, and Gem/Kir (RGK) GTPases, comprise a subfamily of small Ras-related GTP-binding proteins, and have been shown to potently inhibit high voltage-activated Ca(2+) channel current following overexpression. Although the molecular mechanisms underlying RGK-mediated Ca(2+) channel regulation remains controversial, recent studies suggest that(More)
Rem, Rem2, Rad, and Gem/Kir (RGK) represent a distinct GTPase family with largely unknown physiological functions. We report here that both Rem and Rad bind directly to Ca2+ channel beta-subunits (CaV beta) in vivo. No calcium currents are recorded from human embryonic kidney 293 cells coexpressing the L type Ca2+ channel subunits CaV1.2, CaV beta 2a, and(More)
There are twenty-five known inherited cardiac arrhythmia susceptibility genes, all of which encode either ion channel pore-forming subunits or proteins that regulate aspects of ion channel biology such as function, trafficking, and localization. The human KCNE gene family comprises five potassium channel regulatory subunits, sequence variants in each of(More)
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(More)
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