Evidence map›Paper›PMID 11358866›Full record

ArticleGenes & development2001

Yak1p, a DYRK family kinase, translocates to the nucleus and phosphorylates yeast Pop2p in response to a glucose signal.

H Moriya, Y Shimizu-Yoshida, A Omori, S Iwashita, M Katoh, A Sakai

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Article in Genes & development, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

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0cells of the map it votes in
64citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

64 citing papers in PubMed, 145 citations in OpenAlex.

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4 more citing papers are in PubMed but not listed here.

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 at 1 institution in 1 country.

H MoriyaGlucose Signaling Group, Mitsubishi Kasei Institute of Life Sciences, Tokyo 194-8511, Japan.
Y Shimizu-Yoshida
A Omori
S Iwashita
M Katoh
A Sakai
Mitsubishi Group (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

POP2 protein of Saccharomyces cerevisiae is a component of a protein complex that regulates the transcription of many genes. We found that the 97th threonine residue (Thr 97) of Pop2p was phosphorylated upon glucose limitation. The Thr 97 phosphorylation occurred within 2 min after removing glucose and was reversed within 1 min after the readdition of glucose. The effects of hexokinase mutations and glucose analogs indicate that this phosphorylation is dependent on glucose phosphorylating activity. We purified a protein kinase that phosphorylates a peptide containing Thr 97 of Pop2p and identified it as Yak1p, a DYRK family kinase. Phosphorylation of Pop2p was barely detectable in a yak1Delta strain. We found that Yak1p interacted with Bmh1p and Bmh2p only in the presence of glucose. A GFP-Yak1p fusion protein shuttled rapidly between the nucleus and the cytoplasm in response to glucose. A strain with alanine substituted for Thr 97 in Pop2p showed overgrowth in the postdiauxic transition and failed to stop the cell cycle at G(1) phase in response to glucose deprivation. Thus, Yak1p and Pop2p are part of a novel glucose-sensing system in yeast that is involved in growth control in response to glucose availability.

Indexed as

RibonucleasesSaccharomyces cerevisiae ProteinsCarrier ProteinsCell DivisionCell NucleusDyrk KinasesElectrophoresis, Polyacrylamide GelGlucoseIntracellular Signaling Peptides and ProteinsPhosphorylationProtein Serine-Threonine KinasesProtein-Tyrosine KinasesSaccharomyces cerevisiaeSignal TransductionTranscription FactorsCarrier ProteinsDyrk KinasesGlucoseIntracellular Signaling Peptides and ProteinsPOP2 protein, S cerevisiaeProtein Serine-Threonine KinasesProtein-Tyrosine KinasesRibonucleasesSaccharomyces cerevisiae ProteinsTranscription FactorsYAK1 protein, S cerevisiae

Identifiers

PMID11358866
PMCPMC313799
OpenAlexW2156776764

What OpenQuestion holds

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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.