Evidence map›Paper›PMID 12588977›Full record

ArticleMolecular and cellular biology2003

Identification of p21-activated kinase specificity determinants in budding yeast: a single amino acid substitution imparts Ste20 specificity to Cla4.

Megan E Keniry, George F Sprague

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

8 citing papers in PubMed, 15 citations in OpenAlex.

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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.

Megan E KeniryDepartment of Biology and Institute of Molecular Biology, University of Oregon, Eugene, Oregon 97403-1229, USA.
George F Sprague
University of Oregon · US

Funding

Graduate Training in Genetics Administrative Supplement - Career Curriculum DevelopmentT32GM007413 · NIGMS · UNIVERSITY OF OREGON · PI GUILLEMIN, KAREN J · 1985 to 2022
$7.8M
GENETIC REGULATION OF YEAST CELL TYPER01GM030027 · NIGMS · UNIVERSITY OF OREGON · PI SPRAGUE, GEORGE F. · 1985 to 2008
$3.0M
NIGMS NIH HHS GM07413NIGMS NIH HHS GM-30027NIGMS NIH HHS R01 GM030027NIGMS NIH HHS T32 GM007413
6 · The paper itself

Abstract

Two closely related p21-activated kinases from Saccharomyces cerevisiae, Ste20 and Cla4, interact with and are regulated by Cdc42, a small Rho-like GTPase. These kinases are argued to perform a common essential function, based on the observation that the single mutants are viable whereas the double mutant is inviable. Despite having a common upstream regulator and at least one common function, these molecules also have many distinct cellular signaling roles. Ste20 signals upstream of several mitogen-activated protein kinase cascades (e.g., pheromone response, filamentous growth, and high osmolarity), and Cla4 signals during budding and cytokinesis. In order to investigate how these kinases are directed to distinct functions, we sought to identify specificity determinants within Ste20 and Cla4. To this end, we constructed both chimeric fusions and point mutants and tested their ability to perform unique and shared cellular roles. Specificity determinants for both kinases were mapped to the C-terminal kinase domains. Remarkably, the substitution of a single amino acid, threonine 818, from Ste20 into an otherwise wild-type Cla4, Cla4D772T, conferred the ability to perform many Ste20-specific functions.

Indexed as

Saccharomyces cerevisiae Proteinsbeta-GalactosidaseBlotting, WesternGlutathione TransferaseHaploidyIntracellular Signaling Peptides and ProteinsMAP Kinase Kinase Kinasesp21-Activated KinasesPhosphorylationPlasmidsPoint MutationProtein BindingProtein Serine-Threonine KinasesProtein Structure, TertiaryRecombinant Fusion ProteinsSaccharomycetalesbeta-GalactosidaseCLA4 protein, S cerevisiaeGlutathione TransferaseIntracellular Signaling Peptides and ProteinsMAP Kinase Kinase Kinasesp21-Activated KinasesProtein Serine-Threonine KinasesRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSte11 protein, S cerevisiaeSTE20 protein, S cerevisiaeThreonine

Identifiers

PMID12588977
PMCPMC151699
OpenAlexW2089079429

What OpenQuestion holds

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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.