Evidence map›Paper›PMID 21451250›Full record

ArticleJournal of biosciences2011

Requirements of Slm proteins for proper eisosome organization, endocytic trafficking and recycling in the yeast Saccharomyces cerevisiae.

Chitra Kamble, Sandhya Jain, Erin Murphy, Kyoungtae Kim

Abstract read
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In one paragraph

Article in Journal of biosciences, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

21 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Plasma Membrane MCC/Eisosome Domains Promote Stress Resistance in Fungi.Microbiology and molecular biology reviews : MMBR · 2020
    Review
  5. Article
  6. Endocytosis Detection inBio-protocol · 2019
    Article
  7. Review
  8. Analysis of the roles of phosphatidylinositol-4,5-Molecular biology of the cell · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Eisosomes and plasma membrane organization.Molecular genetics and genomics : MGG · 2012
    Review
  18. Review
  19. Article
  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

4 authors at 1 institution in 1 country.

Chitra KambleDepartment of Biology, Missouri State University, 901 South National Ave, Springfield, MO 65897, USA.
Sandhya Jain
Erin Murphy
Kyoungtae Kim
Missouri State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eisosomes are large immobile assemblies at the cortex of a cell under the membrane compartment of Can1 (MCC) in yeast. Slm1 has recently been identified as an MCC component that acts downstream of Mss4 in a pathway that regulates actin cytoskeleton organization in response to stress. In this study, we showed that inactivation of Slm proteins disrupts proper localization of the primary eisosome marker Pil1, providing evidence that Slm proteins play a role in eisosome organization. Furthermore, we found that slm ts mutant cells exhibit actin defects in both the ability to polarize cortical F-actin and the formation of cytoplasmic actin cables even at the permissive temperature (30 degrees C). We further demonstrated that the actin defect accounts for the slow traffic of FM4-64- labelled endosome in the cytoplasm, supporting the notion that intact actin is essential for endosome trafficking. However, our real-time microscopic analysis of Abp1-RFP revealed that the actin defect in slm ts cells was not accompanied by a noticeable defect in actin patch internalization during receptor-mediated endocytosis. In addition, we found that slm ts cells displayed impaired membrane recycling and that recycling occurred in an actin-independent manner. Our data provide evidence for the requirement of Slm proteins in eisosome organization and endosome trafficking and recycling.

Indexed as

ActinsCarrier ProteinsCytoskeletal ProteinsEndosomesMultiprotein ComplexesPhalloidinePhosphoproteinsProtein TransportPyridinium CompoundsQuaternary Ammonium CompoundsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionTime-Lapse ImagingActinsCarrier ProteinsCytoskeletal Proteinsfluorescein isothiocyanate-phalloidinFM 4-64Multiprotein ComplexesPhalloidinePhosphoproteinsPIL1 protein, S cerevisiaePyridinium CompoundsQuaternary Ammonium CompoundsSaccharomyces cerevisiae ProteinsSlm1 protein, S cerevisiae

Identifiers

PMID21451250
OpenAlexW1969789874

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.