Evidence map›Paper›PMID 20230054›Full record

ArticleJournal of the American Chemical Society2010

Sequential rearrangement of interhelical networks upon rhodopsin activation in membranes: the Meta II(a) conformational substate.

Ekaterina Zaitseva, Michael F Brown, Reiner Vogel

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Article
  2. Article
  3. A short story on how chromophore is hydrolyzed from rhodopsin for recycling.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Review
  4. Article
  5. Hydration-mediated G-protein-coupled receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Article
  7. Article
  8. Capturing Peptide-GPCR Interactions and Their Dynamics.Molecules (Basel, Switzerland) · 2020
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. A Usual G-Protein-Coupled Receptor in Unusual Membranes.Angewandte Chemie (International ed. in English) · 2016
    Article
  14. Article
  15. Retinal Flip in Rhodopsin Activation?Biophysical journal · 2015
    Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Deconstructing activation events in rhodopsin.Journal of the American Chemical Society · 2013
    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

3 authors.

Ekaterina ZaitsevaBiophysics Section, Institute of Molecular Medicine and Cell Research, University of Freiburg, Hermann-Herder-Str. 9, D-79104 Freiburg, Germany.
Michael F Brown
Reiner Vogel

Funding

MEMBRANE BASIS OF VISUAL EXCITATIONR01EY012049 · NEI · UNIVERSITY OF ARIZONA · PI BROWN, MICHAEL F · 1998 to 2012
$3.3M
LIPID MODULATION OF RHODOPSIN SIGNALING IN MEMBRANESR01EY018891 · NEI · UNIVERSITY OF ARIZONA · PI BROWN, MICHAEL F · 2008 to 2010
$1.1M
NEI NIH HHS EY012049NEI NIH HHS EY018891NEI NIH HHS R01 EY012049NEI NIH HHS R01 EY018891
6 · The paper itself

Abstract

Photon absorption by rhodopsin is proposed to lead to an activation pathway that is described by the extended reaction scheme Meta I <==>Meta II(a) <==> Meta II(b) <==> Meta II(b)H(+), where Meta II(b)H(+) is thought to be the conformational substate that activates the G protein transducin. Here we test this extended scheme for rhodopsin in a membrane bilayer environment by investigating lipid perturbation of the activation mechanism. We found that symmetric membrane lipids having two unsaturated acyl chains, such as 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC), selectively stabilize the Meta II(a) substate in the above mechanism. By combining FTIR and UV-visible difference spectroscopy, we characterized the structural and functional changes involved in the transition to the Meta II(a) intermediate, which links the inactive Meta I intermediate with the Meta II(b) states formed by helix rearrangement. Besides the opening of the Schiff base ionic lock, the Meta II(a) substate is characterized by an activation switch in a conserved water-mediated hydrogen-bonded network involving transmembrane helices H1/H2/H7, which is sensed by its key residue Asp83. On the other hand, movement of retinal toward H5 and its interaction with another interhelical H3/H5 network mediated by His211 and Glu122 is absent in Meta II(a). The latter rearrangement takes place only in the subsequent transition to Meta II(b), which has been previously associated with movement of H6. Our results imply that activating structural changes in the H1/H2/H7 network are triggered by disruption of the Schiff base salt bridge and occur prior to other chromophore-induced changes in the H3/H5 network and the outward tilt of H6 in the activation process.

Indexed as

AnimalsCattleHeterotrimeric GTP-Binding ProteinsLipid BilayersModels, MolecularPhosphatidylcholinesProtein ConformationRetinaldehydeRhodopsinSchiff Bases1,2-oleoylphosphatidylcholineHeterotrimeric GTP-Binding ProteinsLipid BilayersPhosphatidylcholinesRetinaldehydeRhodopsinSchiff Bases

Identifiers

PMID20230054
PMCPMC2859452

What OpenQuestion holds

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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.