Evidence map›Paper›PMID 19218422›Full record

ArticleEukaryotic cell2009

p21-activated kinases Cla4 and Ste20 regulate vacuole inheritance in Saccharomyces cerevisiae.

Clinton R Bartholomew, Christopher F J Hardy

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

19 citing papers in PubMed, 34 citations in OpenAlex.

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  10. Genome-Wide Screen forG3 (Bethesda, Md.) · 2018
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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

2 authors at 1 institution in 1 country.

Clinton R BartholomewDepartment of Cell and Developmental Biology, Vanderbilt School of Medicine, Nashville, TN 37232-8240, USA.
Christopher F J Hardy
Vanderbilt University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Each time Saccharomyces cerevisiae cells divide they ensure that both the mother and daughter cell inherit a vacuole by actively transporting a portion of the vacuole into the bud. As the mother cell begins budding, a tubular and vesicular segregation structure forms that is transported into the bud by the myosin V motor Myo2, which is bound to the vacuole-specific myosin receptor, Vac17 (41, 59, 70, 79). Upon arriving in the bud the segregation structure is resolved to found the daughter vacuole. The mechanism that regulates segregation structure resolution in a spatially dependent manner is unknown. In addition to resolving the segregation structure, Vac17 is degraded specifically in the bud to provide directionality to vacuole inheritance. It has been proposed that bud-specific degradation of Vac17 is promoted by proteins localized to or activated solely in the bud (77). The p21-activated kinases (PAKs) Cla4 and Ste20 are localized to and activated in the bud. Here we report that Cla4 is localized to the segregation structure just prior to segregation structure resolution, and cells lacking PAK function fail to resolve the segregation structure. Overexpression of either Cla4 or Ste20 inhibited vacuole inheritance and this inhibition was suppressed by the expression of nondegradable VAC17. Finally, PAK activity was required for Vac17 degradation in late M phase and CLA4 overexpression promoted Vac17 degradation. We propose that Cla4 and Ste20 are bud-specific proteins that play roles in both segregation structure resolution and the degradation of Vac17.

Indexed as

CytokinesisGene Expression Regulation, FungalIntracellular Signaling Peptides and ProteinsMAP Kinase Kinase KinasesProtein Serine-Threonine KinasesProtein TransportReceptors, Cell SurfaceSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpecies SpecificityVacuolesVesicular Transport ProteinsCLA4 protein, S cerevisiaeIntracellular Signaling Peptides and ProteinsMAP Kinase Kinase KinasesProtein Serine-Threonine KinasesReceptors, Cell SurfaceSaccharomyces cerevisiae ProteinsSTE20 protein, S cerevisiaeVAC17 protein, S cerevisiaeVesicular Transport Proteins

Identifiers

PMID19218422
PMCPMC2669209
OpenAlexW2122006707

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.