ArticleProceedings of the National Academy of Sciences of the United States of America2003
Regulation of voltage-gated calcium channel activity by the Rem and Rad GTPases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers.
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Who cites it
116 citing papers in PubMed, 211 citations in OpenAlex.
- Molecular Partners of Voltage-Gated Calcium Channel β and αThe Journal of membrane biology · 2026Review
- Direct crosstalk between GPCRs and ion channels via G proteins.Experimental & molecular medicine · 2025Review
- RRAD-reduction reveals efficacy of targeting L-type calcium channel regulation for treatment of heart failure.Cardiovascular research · 2025Article
- Casein Kinase 2 Regulates the Intrinsic Activity of L-Type Calcium Currents in Cardiomyocytes.International journal of molecular sciences · 2025Article
- Pharmacological or genetic inhibition of LTCC promotes cardiomyocyte proliferation through inhibition of calcineurin activity.NPJ Regenerative medicine · 2025Article
- Rad-mediated inhibition of CaThe Journal of physiology · 2024Article
- Tripartite interactions of PKA catalytic subunit and C-terminal domains of cardiac CaBMC biology · 2024Article
- β-adrenergic regulation of CaBiophysics reports · 2024Article
- Rad protein: An essential player in L-type Ca2+ channel localization and modulation in cardiomyocytes.The Journal of general physiology · 2024Article
- The C-terminus of Rad is required for membrane localization and L-type calcium channel regulation.The Journal of general physiology · 2024Article
- A membrane-associated phosphoswitch in Rad controls adrenergic regulation of cardiac calcium channels.The Journal of clinical investigation · 2024Article
- Pharmacological or genetic inhibition of LTCC promotes cardiomyocyte proliferation through inhibition of calcineurin activity.Research square · 2023Article
- Aberrant DJ-1 expression underlies L-type calcium channel hypoactivity in dendrites in tuberous sclerosis complex and Alzheimer's disease.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Phosphodiesterase 8 governs cAMP/PKA-dependent reduction of L-type calcium current in human atrial fibrillation: a novel arrhythmogenic mechanism.European heart journal · 2023Article
- DoxoDB: A Database for the Expression Analysis of Doxorubicin-Induced lncRNA Genes.Non-coding RNA · 2023Article
- The Advantages, Challenges, and Future of Human-Induced Pluripotent Stem Cell Lines in Type 2 Long QT Syndrome.Journal of cardiovascular translational research · 2023Review
- Inactivation influences the extent of inhibition of voltage-gated CaFrontiers in physiology · 2023Article
- Sympathetic Nervous System Regulation of Cardiac Calcium Channels.Handbook of experimental pharmacology · 2023Article
- Genome Editing and Inherited Cardiac Arrhythmias.Advances in experimental medicine and biology · 2023Article
56 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
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 Rem or Rad, but CaV1.2 and CaV beta 2a transfected cells elicit Ca2+ channel currents in the absence of these small G proteins. Importantly, CaV3 (T type) Ca2+ channels, which do not require accessory subunits for ionic current expression, are not inhibited by expression of Rem. Rem is expressed in primary skeletal myoblasts and, when overexpressed in C2C12 myoblasts, wild-type Rem inhibits L type Ca2+ channel activity. Deletion analysis demonstrates a critical role for the Rem C terminus in both regulation of functional Ca2+ channel expression and beta-subunit association. These results suggest that all members of the RGK GTPase family, via direct interaction with auxiliary beta-subunits, serve as regulators of L type Ca2+ channel activity. Thus, the RGK GTPase family may provide a mechanism for achieving cross talk between Ras-related GTPases and electrical signaling pathways.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.