Evidence map›Paper›PMID 19726565›Full record

ArticleMolecular biology of the cell2009

Kei1: a novel subunit of inositolphosphorylceramide synthase, essential for its enzyme activity and Golgi localization.

Keisuke Sato, Yoichi Noda, Koji Yoda

Abstract readComparative Study
In one paragraph

Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

25 citing papers in PubMed.

  1. Article
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  17. The yeast sphingolipid signaling landscape.Chemistry and physics of lipids · 2014
    Review
  18. Article
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  20. Article
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.

Keisuke SatoDepartment of Biotechnology, University of Tokyo, Tokyo 113-8657, Japan.
Yoichi Noda
Koji Yoda

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fungal sphingolipids have inositol-phosphate head groups, which are essential for the viability of cells. These head groups are added by inositol phosphorylceramide (IPC) synthase, and AUR1 has been thought to encode this enzyme. Here, we show that an essential protein encoded by KEI1 is a novel subunit of IPC synthase of Saccharomyces cerevisiae. We find that Kei1 is localized in the medial-Golgi and that Kei1 is cleaved by Kex2, a late Golgi processing endopeptidase; therefore, it recycles between the medial- and late Golgi compartments. The growth defect of kei1-1, a temperature-sensitive mutant, is effectively suppressed by the overexpression of AUR1, and Aur1 and Kei1 proteins form a complex in vivo. The kei1-1 mutant is hypersensitive to aureobasidin A, a specific inhibitor of IPC synthesis, and the IPC synthase activity in the mutant membranes is thermolabile. A part of Aur1 is missorted to the vacuole in kei1-1 cells. We show that the amino acid substitution in kei1-1 causes release of Kei1 during immunoprecipitation of Aur1 and that Aur1 without Kei1 has hardly detectable IPC synthase activity. From these results, we conclude that Kei1 is essential for both the activity and the Golgi localization of IPC synthase.

Indexed as

Amino Acid SequenceCoat Protein Complex IDepsipeptidesGene Expression Regulation, FungalGlycosphingolipidsGolgi ApparatusHexosyltransferasesMembrane LipidsMembrane ProteinsMolecular Sequence DataMultienzyme ComplexesProprotein ConvertasesProtein Interaction MappingProtein Structure, TertiaryRecombinant Fusion ProteinsSaccharomyces cerevisiaeaureobasidin ACoat Protein Complex IDepsipeptidesGlycosphingolipidsHexosyltransferasesinositolphosphorylceramideKei1 protein, S cerevisiaeKEX2 protein, S cerevisiaeMembrane LipidsMembrane ProteinsMultienzyme Complexesphosphatidylinositol-ceramide phosphoinositol transferaseProprotein ConvertasesRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsTransferases (Other Substituted Phosphate Groups)

Identifiers

PMID19726565
PMCPMC2762142

What OpenQuestion holds

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Registered trials

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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.