ArticleBiophysical journal2008
Rem inhibits skeletal muscle EC coupling by reducing the number of functional L-type Ca2+ channels.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
31 citing papers in PubMed.
- Inactivation influences the extent of inhibition of voltage-gated CaFrontiers in physiology · 2023Article
- Into the spotlight: RGK proteins in skeletal muscle.Cell calcium · 2021Review
- Role of High Voltage-Gated CaCells · 2021Review
- Designer genetically encoded voltage-dependent calcium channel inhibitors inspired by RGK GTPases.The Journal of physiology · 2020Review
- A potent voltage-gated calcium channel inhibitor engineered from a nanobody targeted to auxiliary CaeLife · 2019Article
- Similar molecular determinants on Rem mediate two distinct modes of inhibition of CaChannels (Austin, Tex.) · 2016Article
- Genome-Wide Detection of CNVs and Their Association with Meat Tenderness in Nelore Cattle.PloS one · 2016Article
- Functional assessment of three Rem residues identified as critical for interactions with Ca(2+) channel β subunits.Pflugers Archiv : European journal of physiology · 2015Article
- Rectification of muscle and nerve deficits in paralyzed ryanodine receptor type 1 mutant embryos.Developmental biology · 2015Article
- Rem uncouples excitation-contraction coupling in adult skeletal muscle fibers.The Journal of general physiology · 2015Article
- Apparent lack of physical or functional interaction between CaV1.1 and its distal C terminus.The Journal of general physiology · 2015Article
- RGK regulation of voltage-gated calcium channels.Science China. Life sciences · 2015Review
- Differential effects of RGK proteins on L-type channel function in adult mouse skeletal muscle.Biophysical journal · 2014Article
- RGK protein-mediated impairment of slow depolarization- dependent Ca2+ entry into developing myotubes.Channels (Austin, Tex.) · 2014Article
- Structure-function of proteins interacting with the α1 pore-forming subunit of high-voltage-activated calcium channels.Frontiers in physiology · 2014Review
- RGK proteins: fashioning muscle with “Rad” new brakes.Channels (Austin, Tex.) · 2014Article
- Regulation of voltage-dependent calcium channels by RGK proteins.Biochimica et biophysica acta · 2013Review
- Stac3 is a component of the excitation-contraction coupling machinery and mutated in Native American myopathy.Nature communications · 2013Article
- Modification of STIM1 by O-linked N-acetylglucosamine (O-GlcNAc) attenuates store-operated calcium entry in neonatal cardiomyocytes.The Journal of biological chemistry · 2012Article
- Adrenergic signaling controls RGK-dependent trafficking of cardiac voltage-gated L-type Ca2+ channels through PKD1.Circulation research · 2012Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
In skeletal muscle, the L-type voltage-gated Ca(2+) channel (1,4-dihydropyridine receptor) serves as the voltage sensor for excitation-contraction (EC) coupling. In this study, we examined the effects of Rem, a member of the RGK (Rem, Rem2, Rad, Gem/Kir) family of Ras-related monomeric GTP-binding proteins, on the function of the skeletal muscle L-type Ca(2+) channel. EC coupling was found to be weakened in myotubes expressing Rem tagged with enhanced yellow fluorescent protein (YFP-Rem), as assayed by electrically evoked contractions and myoplasmic Ca(2+) transients. This impaired EC coupling was not a consequence of altered function of the type 1 ryanodine receptor, or of reduced Ca(2+) stores, since the application of 4-chloro-m-cresol, a direct type 1 ryanodine receptor activator, elicited myoplasmic Ca(2+) release in YFP-Rem-expressing myotubes that was not distinguishable from that in control myotubes. However, YFP-Rem reduced the magnitude of L-type Ca(2+) current by approximately 75% and produced a concomitant reduction in membrane-bound charge movements. Thus, our results indicate that Rem negatively regulates skeletal muscle EC coupling by reducing the number of functional L-type Ca(2+) channels in the plasma membrane.
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