Evidence map›Paper›PMID 10198054›Full record

ArticleMolecular biology of the cell1999

Uridine diphosphate-glucose transport into the endoplasmic reticulum of Saccharomyces cerevisiae: in vivo and in vitro evidence.

O Castro, L Y Chen, A J Parodi, C Abeijón

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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

16 citing papers in PubMed, 48 citations in OpenAlex.

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  13. Independent and simultaneous translocation of two substrates by a nucleotide sugar transporter.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
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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.

O CastroInstituto de Investigaciones Bioquímicas Fundación Campomar, 1405 Buenos Aires, Argentina.
L Y Chen
A J Parodi
C Abeijón
Boston University · US

Funding

GLYCOSYLATION MECHANISMS OF CELL LIPIDS AND PROTEINSR01GM030365 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI HIRSCHBERG, CARLOS BENJAMIN · 1985 to 2009
$3.1M
TRANSIENT GLUCOSYLATION OF GYLCOPROTEINSR01GM044500 · NIGMS · LELOIR INSTITUTE · PI PARODI, ARMANDO JOSE · 1990 to 2011
$840k
GLYCOSYLATION MECHANISMSR37GM030365 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI HIRSCHBERG, CARLOS BENJAMIN · 1991 to 2000
$365k
NIGMS NIH HHS GM-30365NIGMS NIH HHS GM-44500NIGMS NIH HHS R01 GM030365NIGMS NIH HHS R01 GM044500NIGMS NIH HHS R37 GM030365
6 · The paper itself

Abstract

It has been proposed that synthesis of beta-1,6-glucan, one of Saccharomyces cerevisiae cell wall components, is initiated by a uridine diphosphate (UDP)-glucose-dependent reaction in the lumen of the endoplasmic reticulum (ER). Because this sugar nucleotide is not synthesized in the lumen of the ER, we have examined whether or not UDP-glucose can be transported across the ER membrane. We have detected transport of this sugar nucleotide into the ER in vivo and into ER-containing microsomes in vitro. Experiments with ER-containing microsomes showed that transport of UDP-glucose was temperature dependent and saturable with an apparent Km of 46 microM and a Vmax of 200 pmol/mg protein/3 min. Transport was substrate specific because UDP-N-acetylglucosamine did not enter these vesicles. Demonstration of UDP-glucose transport into the ER lumen in vivo was accomplished by functional expression of Schizosaccharomyces pombe UDP-glucose:glycoprotein glucosyltransferase (GT) in S. cerevisiae, which is devoid of this activity. Monoglucosylated protein-linked oligosaccharides were detected in alg6 or alg5 mutant cells, which transfer Man9GlcNAc2 to protein; glucosylation was dependent on the inhibition of glucosidase II or the disruption of the gene encoding this enzyme. Although S. cerevisiae lacks GT, it contains Kre5p, a protein with significant homology and the same size and subcellular location as GT. Deletion mutants, kre5Delta, lack cell wall beta-1,6 glucan and grow very slowly. Expression of S. pombe GT in kre5Delta mutants did not complement the slow-growth phenotype, indicating that both proteins have different functions in spite of their similarities.

Indexed as

Carbohydrate SequenceEndoplasmic ReticulumGlucosyltransferasesGlycosylationIntracellular MembranesKineticsMolecular Sequence DataOligosaccharidesRecombinant ProteinsReverse Transcriptase Polymerase Chain ReactionSaccharomyces cerevisiaeSchizosaccharomycesSignal TransductionSubstrate SpecificityUridine Diphosphate GlucoseUridine Diphosphate N-AcetylglucosamineGlucosyltransferasesmannosylglycoprotein 1,3-glucosyltransferaseOligosaccharidesRecombinant ProteinsUridine Diphosphate GlucoseUridine Diphosphate N-Acetylglucosamine

Identifiers

PMID10198054
PMCPMC25230
OpenAlexW2170915750

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.