Evidence map›Paper›PMID 16319176›Full record

ArticleMolecular biology of the cell2006

Inositol deacylation by Bst1p is required for the quality control of glycosylphosphatidylinositol-anchored proteins.

Morihisa Fujita, Takehiko Yoko-O, Yoshifumi Jigami

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
2.4field-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

47 citing papers in PubMed, 99 citations in OpenAlex.

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  14. Characterization ofFrontiers in plant science · 2022
    Article
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  19. Endoplasmic Reticulum Export of GPI-Anchored Proteins.International journal of molecular sciences · 2019
    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

3 authors at 2 institutions in 1 country.

Morihisa FujitaResearch Center for Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki 305-8566, Japan.
Takehiko Yoko-O
Yoshifumi Jigami
University of Tsukuba · JPNational Institute of Advanced Industrial Science and Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Misfolded proteins are recognized in the endoplasmic reticulum (ER), transported back to the cytosol, and degraded by the proteasome. A number of proteins are processed and modified by a glycosylphosphatidylinositol (GPI) anchor in the ER, but the quality control mechanisms of GPI-anchored proteins remain unclear. Here, we report on the quality control mechanism of misfolded GPI-anchored proteins. We have constructed a mutant form of the beta-1,3-glucanosyltransferase Gas1p (Gas1*p) as a model misfolded GPI-anchored protein. Gas1*p was modified with a GPI anchor but retained in the ER and was degraded rapidly via the proteasome. Disruption of BST1, which encodes GPI inositol deacylase, caused a delay in the degradation of Gas1*p. This delay was because of an effect on the deacylation activity of Bst1p. Disruption of genes involved in GPI-anchored protein concentration and N-glycan processing caused different effects on the degradation of Gas1*p and a soluble misfolded version of carboxypeptidase Y. Furthermore, Gas1*p associated with both Bst1p and BiP/Kar2p, a molecular chaperone, in vivo. Our data suggest that GPI inositol deacylation plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins.

Indexed as

Protein Processing, Post-TranslationalAcylationEndoplasmic ReticulumGlucan Endo-1,3-beta-D-GlucosidaseGlycosylationGlycosylphosphatidylinositolsInositolMembrane ProteinsMutant ProteinsPhosphoric Monoester HydrolasesProteasome Endopeptidase ComplexProtein FoldingSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteins1,3-beta-glucanosyltransferaseBst1 protein, S cerevisiaeGlucan Endo-1,3-beta-D-GlucosidaseGlycosylphosphatidylinositolsInositolMembrane ProteinsMutant ProteinsPhosphoric Monoester HydrolasesProteasome Endopeptidase ComplexSaccharomyces cerevisiae Proteins

Identifiers

PMID16319176
PMCPMC1356593
OpenAlexW2148658797

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.