Evidence map›Paper›PMID 30975753›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Distinct segregation patterns of yeast cell-peripheral proteins uncovered by a method for protein segregatome analysis.

Shinju Sugiyama, Motomasa Tanaka

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

14 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
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  4. Cell membrane asymmetries and cellular aging.The Biochemical journal · 2025
    Review
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  13. Review
  14. The functional universe of membrane contact sites.Nature reviews. Molecular cell biology · 2020
    Review
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

2 authors at 1 institution in 1 country.

Shinju SugiyamaLaboratory for Protein Conformation Diseases, RIKEN Center for Brain Science, Wako, 351-0198 Saitama, Japan.
Motomasa TanakaLaboratory for Protein Conformation Diseases, RIKEN Center for Brain Science, Wako, 351-0198 Saitama, Japan; motomasa.tanaka@riken.jp.
Tokyo Institute of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein segregation contributes to various cellular processes such as polarization, differentiation, and aging. However, the difficulty in global determination of protein segregation hampers our understanding of its mechanisms and physiological roles. Here, by developing a quantitative proteomics technique, we globally monitored segregation of preexisting and newly synthesized proteins during cell division of budding yeast, and identified crucial domains that determine the segregation of cell-peripheral proteins. Remarkably, the proteomic and subsequent microscopic analyses demonstrated that the flow through the bud neck of the proteins that harbor both endoplasmic reticulum (ER) membrane-spanning and plasma membrane (PM)-binding domains is not restricted by the previously suggested ER membrane or PM diffusion barriers but by septin-mediated partitioning of the PM-associated ER (pmaER). Furthermore, the proteomic analysis revealed that although the PM-spanning t-SNARE Sso2 was retained in mother cells, its paralog Sso1 unexpectedly showed symmetric localization. We found that the transport of Sso1 to buds was required for enhancement of polarized cell growth and resistance to cell-wall stress. Taken together, these data resolve long-standing questions about septin-mediated compartmentalization of the cell periphery, and provide new mechanistic insights into the segregation of cell-periphery proteins and their cellular functions.

Indexed as

Cell CompartmentationCell DivisionCell MembraneCell WallEndoplasmic ReticulumGene Expression Regulation, FungalMembrane ProteinsProtein BindingProtein DomainsProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStress, PhysiologicalMembrane ProteinsSaccharomyces cerevisiae Proteinsasymmetric cell divisionER–PM contact sitepolarized cell growthprotein segregationseptin

Identifiers

PMID30975753
PMCPMC6500170
OpenAlexW2940248057

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.