Evidence map›Paper›PMID 24265205›Full record

ReviewInvestigative ophthalmology & visual science2013

Timing is everything: GTPase regulation in phototransduction.

Vadim Y Arshavsky, Theodore G Wensel

Abstract readReview
In one paragraph

Review in Investigative ophthalmology & visual science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

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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

2 authors.

Vadim Y ArshavskyAlbert Eye Research Institute, Duke University, Durham, North Carolina.
Theodore G Wensel

Funding

VISION RESEARCHP30EY005722 · NEI · DUKE UNIVERSITY · PI Vadim Y Arshavsky · 1985 to 2026
$19.3M
P30 Core Grant for Vision ResearchP30EY014104 · NEI · MASSACHUSETTS EYE AND EAR INFIRMARY · PI Janey L Wiggs · 2002 to 2026
$15.1M
VISION RESEARCH CENTERP30EY002520 · NEI · BAYLOR COLLEGE OF MEDICINE · PI Samuel M Wu · 1985 to 2026
$14.8M
Molecular mechanisms of photoreceptor outer segment morphogenesisR01EY012859 · NEI · MASSACHUSETTS EYE AND EAR INFIRMARY · PI ARSHAVSKY, VADIM Y · 2000 to 2022
$10.0M
Functional Determinnats in G Protein-coupled ReceptorsR01GM066099 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI LICHTARGE, OLIVIER · 2003 to 2022
$7.5M
Transducin movement and photoreceptor light adaptationR01EY010336 · NEI · UNIVERSITY OF WISCONSIN MADISON · PI ARSHAVSKY, VADIM Y · 1994 to 2012
$6.3M
Trasnducin Interactions with Photoreceptor MembranesR01EY007981 · NEI · BAYLOR COLLEGE OF MEDICINE · PI WENSEL, THEODORE G · 1989 to 2016
$6.1M
RGS Protein Function in Mammalian RetinaR01EY011900 · NEI · BAYLOR COLLEGE OF MEDICINE · PI WENSEL, THEODORE G · 1998 to 2010
$4.4M
RGS Domain Function in Mammalian BrainR01DA015189 · NIDA · BAYLOR COLLEGE OF MEDICINE · PI WENSEL, THEODORE G · 2002 to 2006
$1.3M
NEI NIH HHS P30 EY002520NEI NIH HHS P30 EY005722NEI NIH HHS P30 EY014104NEI NIH HHS R01 EY007981NEI NIH HHS R01 EY010336NEI NIH HHS R01 EY011900NEI NIH HHS R01 EY012859NIDA NIH HHS R01 DA015189NIGMS NIH HHS R01 GM066099
6 · The paper itself

Abstract

As the molecular mechanisms of vertebrate phototransduction became increasingly clear in the 1980s, a persistent problem was the discrepancy between the slow GTP hydrolysis catalyzed by the phototransduction G protein, transducin, and the much more rapid physiological recovery of photoreceptor cells from light stimuli. Beginning with a report published in 1989, a series of studies revealed that transducin GTPase activity could approach the rate needed to explain physiological recovery kinetics in the presence of one or more factors present in rod outer segment membranes. One by one, these factors were identified, beginning with PDEγ, the inhibitory subunit of the cGMP phosphodiesterase activated by transducin. There followed the discovery of the crucial role played by the regulator of G protein signaling, RGS9, a member of a ubiquitous family of GTPase-accelerating proteins, or GAPs, for heterotrimeric G proteins. Soon after, the G protein β isoform Gβ5 was identified as an obligate partner subunit, followed by the discovery or R9AP, a transmembrane protein that anchors the RGS9 GAP complex to the disk membrane, and is essential for the localization, stability, and activity of this complex in vivo. The physiological importance of all of the members of this complex was made clear first by knockout mouse models, and then by the discovery of a human visual defect, bradyopsia, caused by an inherited deficiency in one of the GAP components. Further insights have been gained by high-resolution crystal structures of subcomplexes, and by extensive mechanistic studies both in vitro and in animal models.

Indexed as

AnimalsGTP PhosphohydrolasesHumansPhotic StimulationPhotoreceptor Cells, VertebrateVision, OcularGTP Phosphohydrolases

Identifiers

PMID24265205
PMCPMC3837634

What OpenQuestion holds

Textmetadata
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.