Evidence map›Paper›PMID 11294895›Full record

ArticleMolecular biology of the cell2001

The Schizosaccharomyces pombe spo20(+) gene encoding a homologue of Saccharomyces cerevisiae Sec14 plays an important role in forespore membrane formation.

Y Nakase, T Nakamura, A Hirata, S M Routt, H B Skinner, V A Bankaitis, C Shimoda

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

36 citing papers in PubMed, 72 citations in OpenAlex.

  1. Review
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  3. Molecular biology research communications · 2018
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  9. Mfc1 is a novel copper transporter during meiosis.Communicative & integrative biology · 2012
    Article
  10. Review
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  16. 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

7 authors at 3 institutions in 2 countries.

Y NakaseDepartment of Biology, Graduate School of Science, Osaka City University, Sumiyoshi-ku, Osaka 558-8585, Japan.
T Nakamura
A Hirata
S M Routt
H B Skinner
V A Bankaitis
C Shimoda
Osaka City University · JPUniversity of Alabama at Birmingham · USThe University of Tokyo · JP

Funding

Role of the Phospholipids in Golgi Secretory FunctionR01GM044530 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI BANKAITIS, VYTAS A · 1991 to 2019
$5.6M
NIGMS NIH HHS GM44530NIGMS NIH HHS R01 GM044530
6 · The paper itself

Abstract

The Schizosaccharomyces pombe spo20-KC104 mutation was originally isolated in a screen for sporulation-deficient mutants, and the spo20-KC104 mutant exhibits temperature-sensitive growth. Herein, we report that S. pombe, spo20(+) is essential for fission yeast cell viability and is constitutively expressed throughout the life cycle. We also demonstrate that the spo20(+) gene product is structurally homologous to Saccharomyces cerevisiae Sec14, the major phosphatidylinositol transfer protein of budding yeast. This structural homology translates to a significant degree of functional relatedness because reciprocal complementation experiments demonstrate that each protein is able to fulfill the essential function of the other. Moreover, biochemical experiments show that, like Sec14, Spo20 is a phosphatidylinositol/phosphatidylcholine-transfer protein. That Spo20 is required for Golgi secretory function in vegetative cells is indicated by our demonstration that the spo20-KC104 mutant accumulates aberrant Golgi cisternae at restrictive temperatures. However, a second phenotype observed in Spo20-deficient fission yeast is arrest of cell division before completion of cell separation. Consistent with a direct role for Spo20 in controlling cell septation in vegetatively growing cells, localization experiments reveal that Spo20 preferentially localizes to the cell poles and to sites of septation of fission yeast cells. We also report that, when fission yeasts are challenged with nitrogen starvation, Spo20 translocates to the nucleus. This nuclear localization persists during conjugation and meiosis. On completion of meiosis, Spo20 translocates to forespore membranes, and it is the assembly of forespore membranes that is abnormal in spo20-KC104 cells. In such mutants, a considerable fraction of forming prespores fail to encapsulate the haploid nucleus. Our results indicate that Spo20 regulates the formation of specialized membrane structures in addition to its recognized role in regulating Golgi secretory function.

Indexed as

Membrane ProteinsSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsAmino Acid SequenceAnimalsCarrier ProteinsCell SurvivalGenes, FungalGolgi ApparatusHumansMeiosisMolecular Sequence DataMutagenesisPhosphatidylcholinesPhosphatidylinositolsPhospholipid Transfer ProteinsCarrier ProteinsMembrane ProteinsPhosphatidylcholinesPhosphatidylinositolsPhospholipid Transfer ProteinsSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsSEC14 protein, S cerevisiaeSEC24 protein, S cerevisiaeSpo20 protein, S pombe

Identifiers

PMID11294895
PMCPMC32275
OpenAlexW2163802538

What Socratic 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 Socratic graph.