Evidence map›Paper›PMID 17101780›Full record

ArticleMolecular and cellular biology2007

The yeast PH domain proteins Slm1 and Slm2 are targets of sphingolipid signaling during the response to heat stress.

Alexes Daquinag, Maria Fadri, Sung Yun Jung, Jun Qin, Jeannette Kunz

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
–field-weighted citation impact
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

53 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Regulation of sphingolipid synthesis by the G1/S transcription factor Swi4.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2021
    Article
  6. Review
  7. Article
  8. Analysis of the roles of phosphatidylinositol-4,5-Molecular biology of the cell · 2019
    Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
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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

5 authors.

Alexes DaquinagDepartment of Molecular Physiology & Biophysics, Baylor College of Medicine, One Baylor Plaza, BCM335, Houston, TX 77030, USA.
Maria Fadri
Sung Yun Jung
Jun Qin
Jeannette Kunz

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 GM 068098-S1NIGMS NIH HHS R01 GM068098
6 · The paper itself

Abstract

The PH domain-containing proteins Slm1 and Slm2 were previously identified as effectors of the phosphatidylinositol-4,5-bisphosphate (PI4,5P(2)) and TORC2 signaling pathways. Here, we demonstrate that Slm1 and Slm2 are also targets of sphingolipid signaling during the heat shock response. We show that upon depletion of cellular sphingolipid levels, Slm1 function becomes essential for survival under heat stress. We further demonstrate that Slm proteins are regulated by a phosphorylation/dephosphorylation cycle involving the sphingolipid-activated protein kinases Pkh1 and Pkh2 and the calcium/calmodulin-dependent protein phosphatase calcineurin. By using a combination of mass spectrometry and mutational analysis, we identified serine residue 659 in Slm1 as a site of phosphorylation. Characterization of Slm1 mutants that mimic dephosphorylated and phosphorylated states demonstrated that phosphorylation at serine 659 is vital for survival under heat stress and promotes the proper polarization of the actin cytoskeleton. Finally, we present evidence that Slm proteins are also required for the trafficking of the raft-associated arginine permease Can1 to the plasma membrane, a process that requires sphingolipid synthesis and actin polymerization. Together with previous work, our findings suggest that Slm proteins are subject to regulation by multiple signals, including PI4,5P(2), TORC2, and sphingolipids, and may thus integrate inputs from different signaling pathways to temporally and spatially control actin polarization.

Indexed as

3-Phosphoinositide-Dependent Protein KinasesAmino Acid Transport Systems, BasicCalcineurinCarrier ProteinsCell MembraneCytoskeletal ProteinsFatty Acids, MonounsaturatedHeat-Shock ResponseMembrane MicrodomainsPhosphorylationProtein KinasesProtein Serine-Threonine KinasesProtein Structure, TertiaryProtein TransportRNA-Binding ProteinsSaccharomyces cerevisiae3-Phosphoinositide-Dependent Protein KinasesAmino Acid Transport Systems, BasicCalcineurinCAN1 protein, S cerevisiaeCarrier ProteinsCytoskeletal ProteinsFatty Acids, MonounsaturatedPKH1 protein, S cerevisiaePKH2 protein, S cerevisiaeProtein KinasesProtein Serine-Threonine KinasesRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsSlm1 protein, S cerevisiaeSlm2 protein, S cerevisiaeSphingolipidsthermozymocidin

Identifiers

PMID17101780
PMCPMC1800798

What OpenQuestion holds

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Registered trials

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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.