Evidence map›Paper›PMID 8846783›Full record

ArticleThe EMBO journal1995

Fission yeast pak1+ encodes a protein kinase that interacts with Cdc42p and is involved in the control of cell polarity and mating.

S Ottilie, P J Miller, D I Johnson, C L Creasy, M A Sells, S Bagrodia, S L Forsburg, J Chernoff

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
5.3field-weighted citation impact, top 3% 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

57 citing papers in PubMed, 162 citations in OpenAlex.

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  16. Localized activation of p21-activated kinase controls neuronal polarity and morphology.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007
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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

8 authors at 1 institution in 1 country.

S OttilieMolecular Biology and Virology Laboratory, Salk Institute, San Diego, CA 92186, USA.
P J Miller
D I Johnson
C L Creasy
M A Sells
S Bagrodia
S L Forsburg
J Chernoff
Salk Institute for Biological Studies · US

Funding

Viral Vector Core (VVC)P30CA014195 · NCI · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI Ye Zheng · 1985 to 2026
$82.8M
Salk Institute Cancer Training GrantT32CA009370 · NCI · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI Diana Clare Hargreaves, Jan Karlseder · 1986 to 2026
$8.6M
TUMOR-SUPPRESSING PROTEIN-TYROSINE PHOSPHATASER01CA058836 · NCI · RESEARCH INST OF FOX CHASE CAN CTR · PI CHERNOFF, JONATHAN D. · 1993 to 2007
$3.0M
NCI NIH HHS CA-09370NCI NIH HHS CA14195NCI NIH HHS CA58836
6 · The paper itself

Abstract

A STE20/p65pak homolog was isolated from fission yeast by PCR. The pak1+ gene encodes a 72 kDa protein containing a putative p21-binding domain near its amino-terminus and a serine/threonine kinase domain near its carboxyl-terminus. The Pak1 protein autophosphorylates on serine residues and preferentially binds to activated Cdc42p both in vitro and in vivo. This binding is mediated through the p21 binding domain on Pak1p and the effector domain on Cdc42p. Overexpression of an inactive mutant form of pak1 gives rise to cells with markedly abnormal shape with mislocalized actin staining. Pak1 overexpression does not, however, suppress lethality associated with cdc42-null cells or the morphologic defeat caused by overexpression of mutant cdc42 alleles. Gene disruption of pak1+ establishes that, like cdc42+, pak1+ function is required for cell viability. In budding yeast, pak1+ expression restores mating function to STE20-null cells and, in fission yeast, overexpression of an inactive form of Pak inhibits mating. These results indicate that the Pak1 protein is likely to be an effector for Cdc42p or a related GTPase, and suggest that Pak1p is involved in the maintenance of cell polarity and in mating.

Indexed as

Saccharomyces cerevisiae ProteinsActinsAmino Acid SequenceBase Sequencecdc42 GTP-Binding Protein, Saccharomyces cerevisiaeCell Cycle ProteinsCell PolarityCloning, MolecularFungal ProteinsGene Expression Regulation, FungalGenes, FungalGTP-Binding ProteinsGTP PhosphohydrolasesMicroscopy, FluorescenceMolecular Sequence DataMutationActinscdc42 GTP-Binding Protein, Saccharomyces cerevisiaeCell Cycle ProteinsFungal ProteinsGTP-Binding ProteinsGTP PhosphohydrolasesPRK1 protein, S cerevisiaeProtein Serine-Threonine KinasesSaccharomyces cerevisiae Proteins

Identifiers

PMID8846783
PMCPMC394709
OpenAlexW2281196102

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.