Evidence map›Paper›PMID 10397773›Full record

ArticleMolecular biology of the cell1999

A role for Tlg1p in the transport of proteins within the Golgi apparatus of Saccharomyces cerevisiae.

J G Coe, A C Lim, J Xu, W Hong

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

30 citing papers in PubMed, 56 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

J G CoeMembrane Biology Laboratory, Institute of Molecular and Cell Biology, Singapore 117609, Republic of Singapore.
A C Lim
J Xu
W Hong
Institute of Molecular and Cell Biology · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Members of the syntaxin protein family participate in the docking-fusion step of several intracellular vesicular transport events. Tlg1p has been identified as a nonessential protein required for efficient endocytosis as well as the maintenance of normal levels of trans-Golgi network proteins. In this study we independently describe Tlg1p as an essential protein required for cell viability. Depletion of Tlg1p in vivo causes a defect in the transport of the vacuolar protein carboxypeptidase Y through the early Golgi. Temperature-sensitive (ts) mutants of Tlg1p also accumulate the endoplasmic reticulum/cis-Golgi form of carboxypeptidase Y at the nonpermissive temperature (38 degrees C) and exhibit underglycosylation of secreted invertase. Overexpression of Tlg1p complements the growth defect of vti1-11 at the nonpermissive temperature, whereas incomplete complementation was observed with vti1-1, further suggesting a role for Tlg1p in the Golgi apparatus. Overexpression of Sed5p decreases the viability of tlg1 ts mutants compared with wild-type cells, suggesting that tlg1 ts mutants are more susceptible to elevated levels of Sed5p. Tlg1p is able to bind His6-tagged Sec17p (yeast alpha-SNAP) in a dose-dependent manner and enters into a SNARE complex with Vti1p, Tlg2p, and Vps45p. Morphological analyses by electron microscopy reveal that cells depleted of Tlg1p or tlg1 ts mutants incubated at the restrictive temperature accumulate 40- to 50-nm vesicles and experience fragmentation of the vacuole.

Indexed as

Adenosine TriphosphatasesMembrane Transport ProteinsSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsBase Sequencebeta-FructofuranosidaseBiological TransportCarrier ProteinsCell DivisionCloning, MolecularFungal ProteinsGlycoside HydrolasesGolgi ApparatusIntracellular MembranesMembrane ProteinsMolecular Sequence DataAdenosine Triphosphatasesbeta-FructofuranosidaseCarrier ProteinsFungal ProteinsGlycoside HydrolasesMembrane ProteinsMembrane Transport ProteinsQa-SNARE ProteinsQb-SNARE ProteinsSaccharomyces cerevisiae ProteinsSEC17 protein, S cerevisiaeSEC18 protein, S cerevisiaeSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsTLG2 protein, S cerevisiaeVAM3 protein, S cerevisiaeVesicular Transport ProteinsVTI1 protein, S cerevisiae

Identifiers

PMID10397773
PMCPMC25462
OpenAlexW2149062863

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.