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

Citation
H. Moriya et al., Yak1p, a DYRK family kinase, translocates to the nucleus and phosphorylates yeast Pop2p in response to a glucose signal, GENE DEV, 15(10), 2001, pp. 1217-1228
Citations number
40
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Cell & Developmental Biology
Journal title
GENES & DEVELOPMENT
ISSN journal
0890-9369 → ACNP
Volume
15
Issue
10
Year of publication
2001
Pages
1217 - 1228
Database
ISI
SICI code
0890-9369(20010515)15:10<1217:YADFKT>2.0.ZU;2-H
Abstract
POP2 protein of Saccharomyces cerevisiae is a component of a protein comple x that regulates the transcription of many genes. We found that the 97th th reonine residue (Thr 97) of Pop2p was phosphorylated upon glucose limitatio n. 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 phosphorylat ion is dependent on glucose phosphorylating activity. We purified a protein kinase that phosphorylates a peptide containing Thr 97 of Pop2p and identi fied it as Yak1p, a DYRK family kinase. Phosphorylation of Pop2p was barfly detectable in a yak1 Delta strain. We found that Yak1p interacted with Bmh 1p and Bmh2p only in the presence of glucose. A GFP-Yak1p fusion protein sh uttled rapidly between the nucleus and the cytoplasm in response to glucose . A strain with alanine substituted for Thr 97 in Pop2p showed overgrowth i n the postdiauxic transition and failed to stop the cell cycle at G(1) phas e in response to glucose deprivation. Thus, Yak1p and Pop2p are part of a n ovel glucose-sensing system in yeast that is involved in growth control in response to glucose availability.