Evidence map›Paper›PMID 22157956›Full record

ArticleNature structural & molecular biology2011

Intrinsic tethering activity of endosomal Rab proteins.

Sheng-Ying Lo, Christopher L Brett, Rachael L Plemel, Marissa Vignali, Stanley Fields, Tamir Gonen, Alexey J Merz

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.3field-weighted citation impact, top 12% of its field
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

33 citing papers in PubMed, 51 citations in OpenAlex.

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  11. Homotypic and heterotypicThe Journal of biological chemistry · 2019
    Article
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  18. Neuropeptide substance P and the immune response.Cellular and molecular life sciences : CMLS · 2016
    Review
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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

7 authors at 1 institution in 1 country.

Sheng-Ying LoDepartment of Biochemistry, University of Washington School of Medicine, Seattle, Washington, USA.
Christopher L Brett
Rachael L Plemel
Marissa Vignali
Stanley Fields
Tamir Gonen
Alexey J Merz
University of Washington · US

Funding

ZDS2P REGULATES SWE1P-DEPENDENT POLARIZED CELL GROWTH IN S CEREVISIAEP41RR011823 · NCRR · UNIVERSITY OF WASHINGTON · PI DAVIS, TRACY · 1996 to 2011
$24.7M
Dynamics of Endomembrane Docking and FusionR01GM077349 · NIGMS · UNIVERSITY OF WASHINGTON · PI MERZ, ALEXEY JARRELL · 2006 to 2024
$6.1M
Howard Hughes Medical InstituteNCRR NIH HHS P41 RR011823NCRR NIH HHS P41 RR11823NIGMS NIH HHS GM077349NIGMS NIH HHS R01 GM077349
6 · The paper itself

Abstract

Rab small G proteins control membrane trafficking events required for many processes including secretion, lipid metabolism, antigen presentation and growth factor signaling. Rabs recruit effectors that mediate diverse functions including vesicle tethering and fusion. However, many mechanistic questions about Rab-regulated vesicle tethering are unresolved. Using chemically defined reaction systems, we discovered that Vps21, a Saccharomyces cerevisiae ortholog of mammalian endosomal Rab5, functions in trans with itself and with at least two other endosomal Rabs to directly mediate GTP-dependent tethering. Vps21-mediated tethering was stringently and reversibly regulated by an upstream activator, Vps9, and an inhibitor, Gyp1, which were sufficient to drive dynamic cycles of tethering and detethering. These experiments reveal a previously undescribed mode of tethering by endocytic Rabs. In our working model, the intrinsic tethering capacity Vps21 operates in concert with conventional effectors and SNAREs to drive efficient docking and fusion.

Indexed as

EndocytosisEndosomesGTPase-Activating ProteinsGTP-Binding ProteinsGuanine Nucleotide Exchange FactorsGuanosine DiphosphateGuanosine TriphosphateLiposomesMicroscopy, Electron, TransmissionMutationProtein Bindingrab GTP-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSNARE ProteinsTwo-Hybrid System TechniquesGTPase-Activating ProteinsGTP-Binding ProteinsGuanine Nucleotide Exchange FactorsGuanosine DiphosphateGuanosine TriphosphateGYP1 protein, S cerevisiaeLiposomesrab GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsSNARE ProteinsVesicular Transport ProteinsVPS21 protein, S cerevisiaeVPS9 protein, S cerevisiaeYpt10 protein, S cerevisiaeYPT53 protein, S cerevisiae

Identifiers

PMID22157956
PMCPMC3252480
OpenAlexW2113692110

What OpenQuestion holds

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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.