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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2001-5-18
pubmed:abstractText
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.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-10087931, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-10234786, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-10322167, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-10323858, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-10361302, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-10476026, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-10490603, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-10509017, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-10556086, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-10644696, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-10816418, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-1378790, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-1475183, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-2072907, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-2357375, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-2558053, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-2659436, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-326775, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-6310324, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-6336730, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-7732723, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-7744048, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-7791755, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-7857639, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-8368005, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-8887670, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-8939604, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-8975710, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-8985180, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-9312022, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-9428519, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-9472026, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-9495741, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-9504907, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-9564039, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-9584128, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-9813141, http://linkedlifedata.com/resource/pubmed/commentcorrection/11358866-9932450
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Dyrk kinase, http://linkedlifedata.com/resource/pubmed/chemical/Glucose, http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides..., http://linkedlifedata.com/resource/pubmed/chemical/POP2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/YAK1 protein, S cerevisiae
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0890-9369
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1217-28
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Yak1p, a DYRK family kinase, translocates to the nucleus and phosphorylates yeast Pop2p in response to a glucose signal.
pubmed:affiliation
Glucose Signaling Group, Mitsubishi Kasei Institute of Life Sciences, Tokyo 194-8511, Japan.
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