Evidence map›Paper›PMID 16230527›Full record

ArticleGenes & development2005

Bem1p, a scaffold signaling protein, mediates cyclin-dependent control of vacuolar homeostasis in Saccharomyces cerevisiae.

Bong-Kwan Han, Lydia M Bogomolnaya, James M Totten, Heidi M Blank, Lawrence J Dangott, Michael Polymenis

Abstract read
In one paragraph

Article in Genes & development, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Lipid flippases in polarized growth.Current genetics · 2021
    Review
  2. Cellular and metabolic engineering of oleaginous yeastEngineering in life sciences · 2019
    Review
  3. Cell-cycle control of cell polarity in yeast.The Journal of cell biology · 2019
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. The Dcr2p phosphatase destabilizes Sic1p in Saccharomyces cerevisiae.Biochemical and biophysical research communications · 2007
    Article
  15. Article
  16. Article
  17. Article
  18. 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

6 authors.

Bong-Kwan HanDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843, USA.
Lydia M Bogomolnaya
James M Totten
Heidi M Blank
Lawrence J Dangott
Michael Polymenis

Funding

Coordination of Cell Growth with Cell DivisionR01GM062377 · NIGMS · TEXAS A&M UNIVERSITY SYSTEM · PI POLYMENIS, MICHAEL S · 2001 to 2005
$1.1M
NIGMS NIH HHS R01 GM062377NIGMS NIH HHS R01-GM062377
6 · The paper itself

Abstract

How proliferating cells maintain the copy number and overall size of their organelles is not clear. We had previously reported that in the budding yeast Saccharomyces cerevisiae the G1 cyclin Cln3p is required for vacuolar (lysosomal) homotypic fusion and loss of Cln3p leads to vacuolar fragmentation. The Cdc42p GTPase is also required for vacuole fusion. Here we show that the scaffold protein Bem1p, a critical regulator of Cdc42p activity, is a downstream effector of Cln3p and the cyclin-dependent kinase (Cdk) Cdc28p. Our results suggest that Bem1p is phosphorylated in a Cdk-dependent manner to promote vacuole fusion. Replacing Ser72 with Asp, to mimic phosphorylation at an optimal Cdk-consensus site located in the first SH3 domain of Bem1p, suppressed vacuolar fragmentation in cells lacking Cln3p. Using in vivo and in vitro assays, we found that Cln3p was unable to promote vacuole fusion in the absence of Bem1p or in the presence of a nonphosphorylatable Bem1p-Ser72Ala mutant. Furthermore, activation of Cdc42p also suppressed vacuolar fragmentation in the absence of Cln3p. Our results provide a mechanism that links cyclin-dependent kinase activity with vacuole fusion through Bem1p and the Cdc42p GTPase cycle.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SubstitutionCDC28 Protein Kinase, S cerevisiaecdc42 GTP-Binding Protein, Saccharomyces cerevisiaeCyclinsHomeostasisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionVacuolesAdaptor Proteins, Signal TransducingBEM1 protein, S cerevisiaeCDC28 Protein Kinase, S cerevisiaecdc42 GTP-Binding Protein, Saccharomyces cerevisiaeCLN3 protein, S cerevisiaeCyclinsSaccharomyces cerevisiae Proteins

Identifiers

PMID16230527
PMCPMC1276734

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.