Evidence map›Paper›PMID 21094651›Full record

ArticleJournal of molecular biology2011

Asymmetric configurations and N-terminal rearrangements in connexin26 gap junction channels.

Atsunori Oshima, Kazutoshi Tani, Masoud M Toloue, Yoko Hiroaki, Amy Smock, Sayaka Inukai, Angela Cone, Bruce J Nicholson, Gina E Sosinsky, Yoshinori Fujiyoshi

Abstract read
In one paragraph

Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Article
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  7. Article
  8. Conformational changes and COStructure (London, England : 1993) · 2022
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
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  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. Mechanism of gating by calcium in connexin hemichannels.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
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.

Atsunori OshimaDepartment of Biophysics, Faculty of Science, Kyoto University, Oiwake, Kitashirakawa, Sakyo-ku, Kyoto 606-8502, Japan.
Kazutoshi Tani
Masoud M Toloue
Yoko Hiroaki
Amy Smock
Sayaka Inukai
Angela Cone
Bruce J Nicholson
Gina E Sosinsky
Yoshinori Fujiyoshi

Funding

VOLUMETRIC CONTOUR-BASED SURFACE RECONSTRUCTIONP41RR004050 · NCRR · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI PASQUALE, ELENA B · 1989 to 2011
$28.0M
STRUCTURE AND DYNAMICS OF CONNEXIN26 GAP JUNCTIONSR01GM065937 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI PERKINS, GUY A · 2003 to 2016
$3.9M
STRUCTURAL ANALYSIS OF GAP JUNCTION TRAFFICKINGR01GM072881 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI PERKINS, GUY A · 2005 to 2015
$2.6M
SELECTIVE PERMEABILITY &PORE STRUCTURE OF GAP JUNCTIONR01GM055437 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI NICHOLSON, BRUCE J · 1997 to 2009
$2.6M
MECHANISMS OF CONTROL OF CELL GROWTH BY GAP JUNCTIONSR01CA048049 · NCI · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI NICHOLSON, BRUCE J · 1989 to 2003
$1.1M
NCI NIH HHS CA48049NCI NIH HHS R01 CA048049NCRR NIH HHS P41 RR004050NCRR NIH HHS RR04050NIGMS NIH HHS GM065937NIGMS NIH HHS GM072881NIGMS NIH HHS GM55437NIGMS NIH HHS R01 GM055437NIGMS NIH HHS R01 GM065937NIGMS NIH HHS R01 GM072881
6 · The paper itself

Abstract

Gap junction channels are unique in that they possess multiple mechanisms for channel closure, several of which involve the N terminus as a key component in gating, and possibly assembly. Here, we present electron crystallographic structures of a mutant human connexin26 (Cx26M34A) and an N-terminal deletion of this mutant (Cx26M34Adel2-7) at 6-Å and 10-Å resolutions, respectively. The three-dimensional map of Cx26M34A was improved by data from 60° tilt images and revealed a breakdown of the hexagonal symmetry in a connexin hemichannel, particularly in the cytoplasmic domain regions at the ends of the transmembrane helices. The Cx26M34A structure contained an asymmetric density in the channel vestibule ("plug") that was decreased in the Cx26M34Adel2-7 structure, indicating that the N terminus significantly contributes to form this plug feature. Functional analysis of the Cx26M34A channels revealed that these channels are predominantly closed, with the residual electrical conductance showing normal voltage gating. N-terminal deletion mutants with and without the M34A mutation showed no electrical activity in paired Xenopus oocytes and significantly decreased dye permeability in HeLa cells. Comparing this closed structure with the recently published X-ray structure of wild-type Cx26, which is proposed to be in an open state, revealed a radial outward shift in the transmembrane helices in the closed state, presumably to accommodate the N-terminal plug occluding the pore. Because both Cx26del2-7 and Cx26M34Adel2-7 channels are closed, the N terminus appears to have a prominent role in stabilizing the open configuration.

Indexed as

Amino Acid SequenceAnimalsCells, CulturedConnexin 26ConnexinsGap JunctionsHeLa CellsHumansMolecular Sequence DataMutationOocytesProtein ConformationXenopusConnexin 26ConnexinsGJB2 protein, humanGJB2 protein, Xenopus

Identifiers

PMID21094651
PMCPMC3026138

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Registered trials

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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.