Evidence map›Paper›PMID 18799621›Full record

ArticleMolecular biology of the cell2008

The Sur7 protein regulates plasma membrane organization and prevents intracellular cell wall growth in Candida albicans.

Francisco J Alvarez, Lois M Douglas, Adam Rosebrock, James B Konopka

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

55 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
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  7. Article
  8. Sur7 mediates a novel pathway for PIMolecular biology of the cell · 2024
    Article
  9. Article
  10. SUR7 deletion inJournal of extracellular biology · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Plasma Membrane MCC/Eisosome Domains Promote Stress Resistance in Fungi.Microbiology and molecular biology reviews : MMBR · 2020
    Review
  15. Protein markers forJournal of extracellular vesicles · 2020
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Pathogens (Basel, Switzerland) · 2019
    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

4 authors at 1 institution in 1 country.

Francisco J AlvarezDepartment of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, NY 11794-5222, USA.
Lois M Douglas
Adam Rosebrock
James B Konopka
Stony Brook University · US

Funding

Regulation of Morphogenesis in C. albicansR01AI047837 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI James B Konopka · 2001 to 2026
$8.8M
NIAID NIH HHS R01 AI047837NIAID NIH HHS R01 AI47837
6 · The paper itself

Abstract

The Candida albicans plasma membrane plays important roles in cell growth and as a target for antifungal drugs. Analysis of Ca-Sur7 showed that this four transmembrane domain protein localized to stable punctate patches, similar to the plasma membrane subdomains known as eisosomes or MCC that were discovered in S. cerevisiae. The localization of Ca-Sur7 depended on sphingolipid synthesis. In contrast to S. cerevisiae, a C. albicans sur7Delta mutant displayed defects in endocytosis and morphogenesis. Septins and actin were mislocalized, and cell wall synthesis was very abnormal, including long projections of cell wall into the cytoplasm. Several phenotypes of the sur7Delta mutant are similar to the effects of inhibiting beta-glucan synthase, suggesting that the abnormal cell wall synthesis is related to activation of chitin synthase activity seen under stress conditions. These results expand the roles of eisosomes by demonstrating that Sur7 is needed for proper plasma membrane organization and cell wall synthesis. A conserved Cys motif in the first extracellular loop of fungal Sur7 proteins is similar to a characteristic motif of the claudin proteins that form tight junctions in animal cells, suggesting a common role for these tetraspanning membrane proteins in forming specialized plasma membrane domains.

Indexed as

Cell MembraneActinsAmino Acid SequenceCandida albicansCell Cycle ProteinsCell WallCytoskeletal ProteinsEndocytosisFungal ProteinsGene Expression ProfilingHumansHyphaeMembrane ProteinsMolecular Sequence DataMorphogenesisOligonucleotide Array Sequence AnalysisActinsCell Cycle ProteinsCytoskeletal ProteinsFungal ProteinsLSP1 protein, S cerevisiaeMembrane ProteinsPhosphoproteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSUR7 protein, S cerevisiae

Identifiers

PMID18799621
PMCPMC2592640
OpenAlexW2159002698

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.