Evidence map›Paper›PMID 25831508›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

TRAPPII regulates exocytic Golgi exit by mediating nucleotide exchange on the Ypt31 ortholog RabERAB11.

Mario Pinar, Herbert N Arst, Areti Pantazopoulou, Víctor G Tagua, Vivian de los Ríos, Javier Rodríguez-Salarichs, J Fernando Díaz, Miguel A Peñalva

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed.

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  8. Protein expression/secretion boost by a novel unique 21-mer cis-regulatory motif (Exin21) via mRNA stabilization.Molecular therapy : the journal of the American Society of Gene Therapy · 2023
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  15. A Library ofFrontiers in bioengineering and biotechnology · 2021
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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

8 authors.

Mario PinarDepartments of Cellular and Molecular Biology, and.
Herbert N ArstDepartments of Cellular and Molecular Biology, and Section of Microbiology, Imperial College London, London SW7 2AZ, United Kingdom.
Areti PantazopoulouDepartments of Cellular and Molecular Biology, and.
Víctor G TaguaDepartments of Cellular and Molecular Biology, and.
Vivian de los RíosDepartments of Cellular and Molecular Biology, and.
Javier Rodríguez-SalarichsChemical and Physical Biology, Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, 28040 Madrid, Spain; and.ORCID http://orcid.org/0000-0002-2932-0142
J Fernando DíazChemical and Physical Biology, Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, 28040 Madrid, Spain; and.
Miguel A PeñalvaDepartments of Cellular and Molecular Biology, and penalva@cib.csic.es.

Funding

Wellcome TrustWellcome Trust 084660/Z/08/Z
6 · The paper itself

Abstract

The oligomeric complex transport protein particle I (TRAPPI) mediates nucleotide exchange on the RAB GTPase RAB1/Ypt1. TRAPPII is composed of TRAPPI plus three additional subunits, Trs120, Trs130, and Trs65. Unclear is whether TRAPPII mediates nucleotide exchange on RAB1/Ypt1, RAB11/Ypt31, or both. In Aspergillus nidulans, RabO(RAB1) resides in the Golgi, RabE(RAB11) localizes to exocytic post-Golgi carriers undergoing transport to the apex, and hypA encodes Trs120. RabE(RAB11), but not RabO(RAB1), immunoprecipitates contain Trs120/Trs130/Trs65, demonstrating specific association of TRAPPII with RabE(RAB11) in vivo. hypA1(ts) rapidly shifts RabE(RAB11), but not RabO(RAB1), to the cytosol, consistent with HypA(Trs120) being specifically required for RabE(RAB11) activation. Missense mutations rescuing hypA1(ts) at 42 °C mapped to rabE, affecting seven residues. Substitutions in six, of which four resulted in 7- to 36-fold accelerated GDP release, rescued lethality associated to TRAPPII deficiency, whereas equivalent substitutions in RabO(RAB1) did not, establishing that the essential role of TRAPPII is facilitating RabE(RAB11) nucleotide exchange. In vitro, TRAPPII purified with HypA(Trs120)-S-tag accelerates nucleotide exchange on RabE(RAB11) and, paradoxically, to a lesser yet substantial extent, on RabO(RAB1). Evidence obtained by exploiting hypA1-mediated destabilization of HypA(Trs120)/HypC(Trs130)/Trs65 assembly onto the TRAPPI core indicates that these subunits sculpt a second RAB binding site on TRAPP apparently independent from that for RabO(RAB1), which would explain TRAPPII in vitro activity on two RABs. Using A. nidulans in vivo microscopy, we show that HypA(Trs120) colocalizes with RabE(RAB11), arriving at late Golgi cisternae as they dissipate into exocytic carriers. Thus, TRAPPII marks, and possibly determines, the Golgi-to-post-Golgi transition.

Indexed as

Gene Expression Regulation, FungalAspergillus nidulansBinding SitesCytosolEscherichia coliExocytosisFungal ProteinsGlutathione TransferaseGolgi ApparatusGreen Fluorescent ProteinsGuanosine DiphosphateMicroscopy, FluorescenceMutationMutation, MissensePhenotyperab11 GTP-Binding ProteinsFungal ProteinsGlutathione TransferaseGreen Fluorescent ProteinsGuanosine Diphosphaterab11 GTP-Binding Proteinsrab GTP-Binding ProteinsSaccharomyces cerevisiae Proteinstransport protein particle, TRAPPVesicular Transport ProteinsYPT1 protein, S cerevisiaeYPT31 protein, S cerevisiaeAspergillusGEFGolgiGTPasepost-Golgi carriers

Identifiers

PMID25831508
PMCPMC4394270

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.