ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2005
Expression of Rem2, an RGK family small GTPase, reduces N-type calcium current without affecting channel surface density.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 94 citations in OpenAlex.
- Molecular Partners of Voltage-Gated Calcium Channel β and αThe Journal of membrane biology · 2026Review
- The C-terminus of Rad is required for membrane localization and L-type calcium channel regulation.The Journal of general physiology · 2024Article
- Rem2 interacts with CaMKII at synapses and restricts long-term potentiation in hippocampus.bioRxiv : the preprint server for biology · 2024Article
- Rem2 interacts with CaMKII at synapses and restricts long-term potentiation in hippocampus.PloS one · 2024Article
- Design and Applications of Genetically-Encoded Voltage-Dependent Calcium Channel Inhibitors.Handbook of experimental pharmacology · 2023Review
- Inactivation influences the extent of inhibition of voltage-gated CaFrontiers in physiology · 2023Article
- 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
- Article
- Rem2 signaling affects neuronal structure and function in part by regulation of gene expression.Molecular and cellular neurosciences · 2017Article
- Localization of rem2 in the central nervous system of the adult rainbow trout (Oncorhynchus mykiss).Journal of chemical neuroanatomy · 2016Article
- Similar molecular determinants on Rem mediate two distinct modes of inhibition of CaChannels (Austin, Tex.) · 2016Article
- Defining the MO's of RGK proteins.Channels (Austin, Tex.) · 2016Article
- Rad and Rem are non-canonical G-proteins with respect to the regulatory role of guanine nucleotide binding in Ca(V)1.2 channel regulation.The Journal of physiology · 2015Article
- Functional assessment of three Rem residues identified as critical for interactions with Ca(2+) channel β subunits.Pflugers Archiv : European journal of physiology · 2015Article
- Solution NMR and calorimetric analysis of Rem2 binding to the Ca2+ channel β4 subunit: a low affinity interaction is required for inhibition of Cav2.1 Ca2+ currents.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
- Nerve injury induces a Gem-GTPase-dependent downregulation of P/Q-type Ca2+ channels contributing to neurite plasticity in dorsal root ganglion neurons.Pflugers Archiv : European journal of physiology · 2015Article
- RGK regulation of voltage-gated calcium channels.Science China. Life sciences · 2015Review
- Molecular mechanisms of activity-dependent changes in dendritic morphology: role of RGK proteins.Trends in neurosciences · 2014Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Rad, Gem/Kir, Rem, and Rem2 are members of the Ras-related RGK (Rad, Gem, and Kir) family of small GTP-binding proteins. Heterologous expression of RGK proteins interferes with de novo calcium channel assembly/trafficking and dramatically decreases the amplitude of currents arising from preexisting high-voltage-activated calcium channels. These effects probably result from the direct interaction of RGK proteins with calcium channel beta subunits. Among the RGK family, Rem2 is the only member abundantly expressed in neuronal tissues. Here, we examined the ability of Rem2 to modulate endogenous voltage-activated calcium channels in rat sympathetic and dorsal root ganglion neurons. Heterologous expression of Rem2 nearly abolished calcium currents arising from preexisting high-voltage-activated calcium channels without affecting low-voltage-activated calcium channels. Rem2 inhibition of N-type calcium channels required both the Ras homology (core) domain and the polybasic C terminus. Mutation of a putative GTP/Mg2+ binding motif in Rem2 did not affect suppression of calcium currents. Loading neurons with GDP-beta-S via the patch pipette did not reverse Rem2-mediated calcium channel inhibition. Finally, [(125)I]Tyr22-omega-conotoxin GVIA cell surface binding in tsA201 cells stably expressing N-type calcium channels was not altered by Rem2 expression at a time when calcium current was totally abolished. Together, our results support a model in which Rem2 localizes to the plasma membrane via a C-terminal polybasic motif and interacts with calcium channel beta subunits in the preassembled N-type channel, thereby forming a nonconducting species.
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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.