ArticleProceedings of the National Academy of Sciences of the United States of America2001
Control of gating mode by a single amino acid residue in transmembrane segment IS3 of the N-type Ca2+ channel.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
13 citing papers in PubMed, 32 citations in OpenAlex.
- Article
- Voltage-dependent G-protein regulation of CaScience advances · 2024Article
- Molecular insights into the gating mechanisms of voltage-gated calcium channel CaNature communications · 2023Article
- Modulation of voltage-gated CaChannels (Austin, Tex.) · 2020Review
- Fast Inactivation of CaJournal of molecular neuroscience : MN · 2017Article
- (R)-roscovitine prolongs the mean open time of unitary N-type calcium channel currents.Neuroscience · 2010Article
- Decoding of synaptic voltage waveforms by specific classes of recombinant high-threshold Ca(2+) channels.The Journal of physiology · 2003Article
- Neurosteroids shift partial agonist activation of GABA(A) receptor channels from low- to high-efficacy gating patterns.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003Article
- The familial hemiplegic migraine mutation R192Q reduces G-protein-mediated inhibition of P/Q-type (Ca(V)2.1) calcium channels expressed in human embryonic kidney cells.The Journal of physiology · 2003Article
- Alternative splicing of a beta4 subunit proline-rich motif regulates voltage-dependent gating and toxin block of Cav2.1 Ca2+ channels.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2002Article
- Identification and characterization of novel human Ca(v)2.2 (alpha 1B) calcium channel variants lacking the synaptic protein interaction site.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2002Article
- Allosteric modulation of Ca2+ channels by G proteins, voltage-dependent facilitation, protein kinase C, and Ca(v)beta subunits.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- G protein modulation of CaV2 voltage-gated calcium channels.Channels (Austin, Tex.)Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
N-type Ca(2+) channels can be inhibited by neurotransmitter-induced release of G protein betagamma subunits. Two isoforms of Ca(v)2.2 alpha1 subunits of N-type calcium channels from rat brain (Ca(v)2.2a and Ca(v)2.2b; initially termed rbB-I and rbB-II) have different functional properties. Unmodulated Ca(v)2.2b channels are in an easily activated "willing" (W) state with fast activation kinetics and no prepulse facilitation. Activating G proteins shifts Ca(v)2.2b channels to a difficult to activate "reluctant" (R) state with slow activation kinetics; they can be returned to the W state by strong depolarization resulting in prepulse facilitation. This contrasts with Ca(v)2.2a channels, which are tonically in the R state and exhibit strong prepulse facilitation. Activating or inhibiting G proteins has no effect. Thus, the R state of Ca(v)2.2a and its reversal by prepulse facilitation are intrinsic to the channel and independent of G protein modulation. Mutating G177 in segment IS3 of Ca(v)2.2b to E as in Ca(v)2.2a converts Ca(v)2.2b tonically to the R state, insensitive to further G protein modulation. The converse substitution in Ca(v)2.2a, E177G, converts it to the W state and restores G protein modulation. We propose that negatively charged E177 in IS3 interacts with a positive charge in the IS4 voltage sensor when the channel is closed and produces the R state of Ca(v)2.2a by a voltage sensor-trapping mechanism. G protein betagamma subunits may produce reluctant channels by a similar molecular mechanism.
Indexed as
Identifiers
What OpenQuestion holds
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.