Evidence map›Paper›PMID 19356589›Full record

ArticleJournal of molecular biology2009

CLIC2-RyR1 interaction and structural characterization by cryo-electron microscopy.

Xing Meng, Guoliang Wang, Cedric Viero, Qiongling Wang, Wei Mi, Xiao-Dong Su, Terence Wagenknecht, Alan J Williams, Zheng Liu, Chang-Cheng Yin

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.2field-weighted citation impact, top 8% of its field
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

24 citing papers in PubMed, 51 citations in OpenAlex.

  1. Biomolecules · 2023
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  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. A guide to the 3D structure of the ryanodine receptor type 1 by cryoEM.Protein science : a publication of the Protein Society · 2017
    Review
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  10. Article
  11. Article
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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

10 authors at 4 institutions in 3 countries.

Xing MengWadsworth Center, New York State Department of Health, Albany, NY 12201, USA.
Guoliang Wang
Cedric Viero
Qiongling Wang
Wei Mi
Xiao-Dong Su
Terence Wagenknecht
Alan J Williams
Zheng Liu
Chang-Cheng Yin
Peking University · CNCardiff University · GBNew York State Department of Health · USWadsworth Center · US

Funding

ZERNIKE PHASE-CONTRAST IMAGINGP41RR001219 · NCRR · WADSWORTH CENTER · PI WAGENKNECHT, TERENCE C · 1985 to 2010
$11.1M
STRUCTURE OF CHANNELS IN EXCITATION/CONTRACTION COUPLINGR01AR040615 · NIAMS · WADSWORTH CENTER · PI WAGENKNECHT, TERENCE C · 1991 to 2014
$5.6M
British Heart FoundationNCRR NIH HHS P41 RR001219NCRR NIH HHS RR01219NIAMS NIH HHS AR40615NIAMS NIH HHS R01 AR040615
6 · The paper itself

Abstract

Chloride intracellular channel 2 (CLIC2), a newly discovered small protein distantly related to the glutathione transferase (GST) structural family, is highly expressed in cardiac and skeletal muscle, although its physiological function in these tissues has not been established. In the present study, [3H]ryanodine binding, Ca2+ efflux from skeletal sarcoplasmic reticulum (SR) vesicles, single channel recording, and cryo-electron microscopy were employed to investigate whether CLIC2 can interact with skeletal ryanodine receptor (RyR1) and modulate its channel activity. We found that: (1) CLIC2 facilitated [3H]ryanodine binding to skeletal SR and purified RyR1, by increasing the binding affinity of ryanodine for its receptor without significantly changing the apparent maximal binding capacity; (2) CLIC2 reduced the maximal Ca2+ efflux rate from skeletal SR vesicles; (3) CLIC2 decreased the open probability of RyR1 channel, through increasing the mean closed time of the channel; (4) CLIC2 bound to a region between domains 5 and 6 in the clamp-shaped region of RyR1; (5) and in the same clamp region, domains 9 and 10 became separated after CLIC2 binding, indicating CLIC2 induced a conformational change of RyR1. These data suggest that CLIC2 can interact with RyR1 and modulate its channel activity. We propose that CLIC2 functions as an intrinsic stabilizer of the closed state of RyR channels.

Indexed as

Cryoelectron MicroscopyAnimalsCalciumChloride ChannelsCrystallography, X-RayIon Channel GatingModels, MolecularMuscle, SkeletalProtein BindingProtein ConformationRabbitsRyanodine Receptor Calcium Release ChannelSarcoplasmic ReticulumSurface PropertiesTritiumCalciumChloride ChannelsRyanodine Receptor Calcium Release ChannelTritium

Identifiers

PMID19356589
PMCPMC2667806
OpenAlexW1963641571

What OpenQuestion holds

Textmetadata
LicenceTDM
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.