Evidence map›Paper›PMID 20452978›Full record

ArticleThe Journal of biological chemistry2010

Rab3-interacting molecule gamma isoforms lacking the Rab3-binding domain induce long lasting currents but block neurotransmitter vesicle anchoring in voltage-dependent P/Q-type Ca2+ channels.

Yoshitsugu Uriu, Shigeki Kiyonaka, Takafumi Miki, Masakuni Yagi, Satoshi Akiyama, Emiko Mori, Akito Nakao, Aaron M Beedle, Kevin P Campbell, Minoru Wakamori and 1 more

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

28 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. RIM CNeuron · 2018
    Article
  8. Article
  9. C-terminal splice variants of P/Q-type CaThe Journal of biological chemistry · 2017
    Article
  10. Article
  11. The role of laminins in the organization and function of neuromuscular junctions.Matrix biology : journal of the International Society for Matrix Biology · 2017
    Review
  12. Article
  13. Article
  14. Review
  15. RIM3γ and RIM4γ are key regulators of neuronal arborization.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  16. Article
  17. Review
  18. RIM genes differentially contribute to organizing presynaptic release sites.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  19. Review
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors.

Yoshitsugu UriuDepartment of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Kyoto 615-8510, Japan.
Shigeki Kiyonaka
Takafumi Miki
Masakuni Yagi
Satoshi Akiyama
Emiko Mori
Akito Nakao
Aaron M Beedle
Kevin P Campbell
Minoru Wakamori
Yasuo Mori

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Assembly of voltage-dependent Ca(2+) channels (VDCCs) with their associated proteins regulates the coupling of VDCCs with upstream and downstream cellular events. Among the four isoforms of the Rab3-interacting molecule (RIM1 to -4), we have previously reported that VDCC beta-subunits physically interact with the long alpha isoform of the presynaptic active zone scaffolding protein RIM1 (RIM1alpha) via its C terminus containing the C(2)B domain. This interaction cooperates with RIM1alpha-Rab3 interaction to support neurotransmitter exocytosis by anchoring vesicles in the vicinity of VDCCs and by maintaining depolarization-triggered Ca(2+) influx as a result of marked inhibition of voltage-dependent inactivation of VDCCs. However, physiological functions have not yet been elucidated for RIM3 and RIM4, which exist only as short gamma isoforms (gamma-RIMs), carrying the C-terminal C(2)B domain common to RIMs but not the Rab3-binding region and other structural motifs present in the alpha-RIMs, including RIM1alpha. Here, we demonstrate that gamma-RIMs also exert prominent suppression of VDCC inactivation via direct binding to beta-subunits. In the pheochromocytoma PC12 cells, this common functional feature allows native RIMs to enhance acetylcholine secretion, whereas gamma-RIMs are uniquely different from alpha-RIMs in blocking localization of neurotransmitter-containing vesicles near the plasma membrane. Gamma-RIMs as well as alpha-RIMs show wide distribution in central neurons, but knockdown of gamma-RIMs attenuated glutamate release to a lesser extent than that of alpha-RIMs in cultured cerebellar neurons. The results suggest that sustained Ca(2+) influx through suppression of VDCC inactivation by RIMs is a ubiquitous property of neurons, whereas the extent of vesicle anchoring to VDCCs at the plasma membrane may depend on the competition of alpha-RIMs with gamma-RIMs for VDCC beta-subunits.

Indexed as

AnimalsBrainCalcium Channels, N-TypeCricetinaeElectrophysiologyExocytosisHumansMiceMice, Inbred C57BLModels, BiologicalNeuronsNeurotransmitter AgentsPC12 Cellsrab3 GTP-Binding ProteinsRatsSynaptic TransmissionCalcium Channels, N-TypeNeurotransmitter Agentsrab3 GTP-Binding Proteins

Identifiers

PMID20452978
PMCPMC2898395

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.