Evidence map›Paper›PMID 24292832›Full record

ArticleHandbook of experimental pharmacology2014

Self-association of arrestin family members.

Qiuyan Chen, Ya Zhuo, Miyeon Kim, Susan M Hanson, Derek J Francis, Sergey A Vishnivetskiy, Christian Altenbach, Candice S Klug, Wayne L Hubbell, Vsevolod V Gurevich

Abstract read
In one paragraph

Article in Handbook of experimental pharmacology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Structure and self-association of Arrestin-1.Journal of structural biology · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. GPCR targeting of E3 ubiquitin ligase MDM2 by inactive β-arrestin.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Targeting arrestin interactions with its partners for therapeutic purposes.Advances in protein chemistry and structural biology · 2020
    Review
  16. Review
  17. Article
  18. Review
  19. 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.

Qiuyan ChenDepartment of Pharmacology, Vanderbilt University, 2200 Pierce Avenue, Nashville, TN, 37232, USA.
Ya Zhuo
Miyeon Kim
Susan M Hanson
Derek J Francis
Sergey A Vishnivetskiy
Christian Altenbach
Candice S Klug
Wayne L Hubbell
Vsevolod V Gurevich

Funding

Vision Research Core at UCLAP30EY000331 · NEI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Xian-Jie Yang · 1985 to 2026
$16.8M
STRUCTURE/FUNCTION STUDIES OF VISUAL ARRESTINR01EY011500 · NEI · VANDERBILT UNIVERSITY · PI T M Iverson · 1997 to 2026
$12.3M
MOLECULAR BASIS OF MEMBRANE EXCITATIONR01EY005216 · NEI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HUBBELL, WAYNE L · 1985 to 2019
$9.8M
Arrestin interactions with non-receptor binding partnersR01GM077561 · NIGMS · VANDERBILT UNIVERSITY · PI GUREVICH, VSEVOLOD V. · 2007 to 2015
$2.3M
Spin Labeling of MsbAR01GM070642 · NIGMS · MEDICAL COLLEGE OF WISCONSIN · PI KLUG, CANDICE S · 2004 to 2012
$1.9M
NEI NIH HHS P30 EY000331NEI NIH HHS R01 EY005216NEI NIH HHS R01 EY011500NIGMS NIH HHS R01 GM070642NIGMS NIH HHS R01 GM077561
6 · The paper itself

Abstract

Mammals express four arrestin subtypes, three of which have been shown to self-associate. Cone photoreceptor-specific arrestin-4 is the only one that is a constitutive monomer. Visual arrestin-1 forms tetramers both in crystal and in solution, but the shape of its physiologically relevant solution tetramer is very different from that in the crystal. The biological role of the self-association of arrestin-1, expressed at very high levels in rod and cone photoreceptors, appears to be protective, reducing the concentration of cytotoxic monomers. The two nonvisual arrestin subtypes are highly homologous, and self-association of both is facilitated by IP6, yet they form dramatically different oligomers. Arrestin-2 apparently self-associates into "infinite" chains, very similar to those observed in IP6-soaked crystals, where IP6 connects the concave sides of the N- and C-domains of adjacent protomers. In contrast, arrestin-3 only forms dimers, in which IP6 likely connects the C-domains of two arrestin-3 molecules. Thus, each of the three self-associating arrestins does it in its own way, forming three different types of oligomers. The physiological role of the oligomerization of arrestin-1 and both nonvisual arrestins might be quite different, and in each case it remains to be definitively elucidated.

Indexed as

AnimalsArrestinsCrystallizationHumansPhytic AcidProtein MultimerizationRetinal Cone Photoreceptor CellsRetinal Rod Photoreceptor CellsArrestinsPhytic Acid

Identifiers

PMID24292832
PMCPMC4512752

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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.