| Home > Publications Database > Higher-order architecture of rhodopsin in intact photoreceptors and its implication for phototransduction kinetics. > print |
| 001 | 137875 | ||
| 005 | 20240321220331.0 | ||
| 024 | 7 | _ | |a 10.1016/j.str.2015.01.015 |2 doi |
| 024 | 7 | _ | |a pmid:25728926 |2 pmid |
| 024 | 7 | _ | |a 0969-2126 |2 ISSN |
| 024 | 7 | _ | |a 1878-4186 |2 ISSN |
| 024 | 7 | _ | |a altmetric:3740142 |2 altmetric |
| 037 | _ | _ | |a DZNE-2020-04197 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 540 |
| 100 | 1 | _ | |a Gunkel, Monika |b 0 |
| 245 | _ | _ | |a Higher-order architecture of rhodopsin in intact photoreceptors and its implication for phototransduction kinetics. |
| 260 | _ | _ | |a Cambridge, Mass. |c 2015 |b Cell Press |
| 264 | _ | 1 | |3 print |2 Crossref |b Elsevier BV |c 2015-04-01 |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1590667020_3565 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a The visual pigment rhodopsin belongs to the family of G protein-coupled receptors that can form higher oligomers. It is controversial whether rhodopsin forms oligomers and whether oligomers are functionally relevant. Here, we study rhodopsin organization in cryosections of dark-adapted mouse rod photoreceptors by cryoelectron tomography. We identify four hierarchical levels of organization. Rhodopsin forms dimers; at least ten dimers form a row. Rows form pairs (tracks) that are aligned parallel to the disk incisures. Particle-based simulation shows that the combination of tracks with fast precomplex formation, i.e. rapid association and dissociation between inactive rhodopsin and the G protein transducin, leads to kinetic trapping: rhodopsin first activates transducin from its own track, whereas recruitment of transducin from other tracks proceeds more slowly. The trap mechanism could produce uniform single-photon responses independent of rhodopsin lifetime. In general, tracks might provide a platform that coordinates the spatiotemporal interaction of signaling molecules. |
| 536 | _ | _ | |a 341 - Molecular Signaling (POF3-341) |0 G:(DE-HGF)POF3-341 |c POF3-341 |f POF III |x 0 |
| 542 | _ | _ | |i 2015-04-01 |2 Crossref |u https://www.elsevier.com/tdm/userlicense/1.0/ |
| 542 | _ | _ | |i 2016-04-07 |2 Crossref |u https://www.elsevier.com/open-access/userlicense/1.0/ |
| 588 | _ | _ | |a Dataset connected to CrossRef, PubMed, |
| 650 | _ | 7 | |a Rhodopsin |0 9009-81-8 |2 NLM Chemicals |
| 650 | _ | 7 | |a Transducin |0 EC 3.6.5.1 |2 NLM Chemicals |
| 650 | _ | 2 | |a Animals |2 MeSH |
| 650 | _ | 2 | |a Kinetics |2 MeSH |
| 650 | _ | 2 | |a Mice |2 MeSH |
| 650 | _ | 2 | |a Mice, Inbred C57BL |2 MeSH |
| 650 | _ | 2 | |a Photoreceptor Cells: metabolism |2 MeSH |
| 650 | _ | 2 | |a Photoreceptor Cells: ultrastructure |2 MeSH |
| 650 | _ | 2 | |a Protein Binding |2 MeSH |
| 650 | _ | 2 | |a Protein Multimerization |2 MeSH |
| 650 | _ | 2 | |a Rhodopsin: chemistry |2 MeSH |
| 650 | _ | 2 | |a Rhodopsin: metabolism |2 MeSH |
| 650 | _ | 2 | |a Transducin: metabolism |2 MeSH |
| 650 | _ | 2 | |a Vision, Ocular |2 MeSH |
| 700 | 1 | _ | |a Schöneberg, Johannes |b 1 |
| 700 | 1 | _ | |a Alkhaldi, Weaam |0 P:(DE-2719)2810249 |b 2 |u dzne |
| 700 | 1 | _ | |a Irsen, Stephan |b 3 |
| 700 | 1 | _ | |a Noé, Frank |b 4 |
| 700 | 1 | _ | |a Kaupp, U Benjamin |0 P:(DE-HGF)0 |b 5 |e Corresponding author |
| 700 | 1 | _ | |a Alamoudi, Ashraf |0 P:(DE-2719)2259138 |b 6 |e Last author |u dzne |
| 773 | 1 | 8 | |a 10.1016/j.str.2015.01.015 |b : Elsevier BV, 2015-04-01 |n 4 |p 628-638 |3 journal-article |2 Crossref |t Structure |v 23 |y 2015 |x 0969-2126 |
| 773 | _ | _ | |a 10.1016/j.str.2015.01.015 |g Vol. 23, no. 4, p. 628 - 638 |0 PERI:(DE-600)2031189-8 |n 4 |q 23:4<628 - 638 |p 628-638 |t Structure |v 23 |y 2015 |x 0969-2126 |
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