Evidence map›Paper›PMID 15689497›Full record

ArticleMolecular biology of the cell2005

The pleckstrin homology domain proteins Slm1 and Slm2 are required for actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5-bisphosphate and TORC2.

Maria Fadri, Alexes Daquinag, Shimei Wang, Tao Xue, Jeannette Kunz

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

79 citing papers in PubMed, 129 citations in OpenAlex.

  1. Article
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  9. Review
  10. Article
  11. Plasma Membrane MCC/Eisosome Domains Promote Stress Resistance in Fungi.Microbiology and molecular biology reviews : MMBR · 2020
    Review
  12. Review
  13. Analysis of the roles of phosphatidylinositol-4,5-Molecular biology of the cell · 2019
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Protein kinase C and calcineurin cooperatively mediate cell survival under compressive mechanical stress.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  20. Review

19 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Maria FadriDepartment of Molecular Physiology and Biophysics, Baylor College of Medicine, Houston, TX 77030, USA.
Alexes Daquinag
Shimei Wang
Tao Xue
Jeannette Kunz
Baylor College of Medicine · US

Funding

Dynamics of phosphoinositide signaling in cell motilityR01GM068098 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI KUNZ, JEANNETTE · 2003 to 2007
$1.3M
NIGMS NIH HHS GM-068098NIGMS NIH HHS R01 GM068098
6 · The paper itself

Abstract

Phosphatidylinositol-4,5-bisphosphate [PtdIns(4,5)P(2)] is a key second messenger that regulates actin and membrane dynamics, as well as other cellular processes. Many of the effects of PtdIns(4,5)P(2) are mediated by binding to effector proteins that contain a pleckstrin homology (PH) domain. Here, we identify two novel effectors of PtdIns(4,5)P(2) in the budding yeast Saccharomyces cerevisiae: the PH domain containing protein Slm1 and its homolog Slm2. Slm1 and Slm2 serve redundant roles essential for cell growth and actin cytoskeleton polarization. Slm1 and Slm2 bind PtdIns(4,5)P(2) through their PH domains. In addition, Slm1 and Slm2 physically interact with Avo2 and Bit61, two components of the TORC2 signaling complex, which mediates Tor2 signaling to the actin cytoskeleton. Together, these interactions coordinately regulate Slm1 targeting to the plasma membrane. Our results thus identify two novel effectors of PtdIns(4,5)P(2) regulating cell growth and actin organization and suggest that Slm1 and Slm2 integrate inputs from the PtdIns(4,5)P(2) and TORC2 to modulate polarized actin assembly and growth.

Indexed as

1-Phosphatidylinositol 4-KinaseActinsAmino Acid SequenceBlood ProteinsCarrier Proteinscdc42 GTP-Binding Protein, Saccharomyces cerevisiaeCell MembraneCytoskeletal ProteinsCytoskeletonMolecular Sequence DataMutationPhosphatidylinositol 4,5-DiphosphatePhosphoproteinsPhosphotransferasesPhosphotransferases (Alcohol Group Acceptor)Protein Binding1-Phosphatidylinositol 4-KinaseActinsBlood ProteinsCarrier Proteinscdc42 GTP-Binding Protein, Saccharomyces cerevisiaeCytoskeletal ProteinsMSS4 protein, S cerevisiaePhosphatidylinositol 4,5-DiphosphatePhosphoproteinsPhosphotransferasesPhosphotransferases (Alcohol Group Acceptor)PKC1 protein, S cerevisiaeplatelet protein P47Protein Kinase CRHO1 protein, S cerevisiaerho GTP-Binding ProteinsRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsSlm1 protein, S cerevisiaeSlm2 protein, S cerevisiaeSTT4 protein, S cerevisiae

Identifiers

PMID15689497
PMCPMC1073669
OpenAlexW2159928898

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.