RapamycinFungusV1, Main, Exploration, bibRecord, 001146

PAS kinase promotes cell survival and growth through activation of Rho1.

Identifieur interne : 001146 ( Main/Exploration ); précédent : 001145; suivant : 001147

PAS kinase promotes cell survival and growth through activation of Rho1.

Auteurs : Caleb M. Cardon [États-Unis] ; Thomas Beck ; Michael N. Hall ; Jared Rutter

Source :

Science signaling [ 1937-9145 ] ; 2012.

RBID : pubmed:22296835

Descripteurs français

KwdFr :
- Activation enzymatique (génétique), Facteurs d'échange de nucléotides guanyliques (génétique), Facteurs d'échange de nucléotides guanyliques (métabolisme), Glucose (génétique), Glucose (métabolisme), Mutation (MeSH), Phosphatidylinositol 3-kinases (génétique), Phosphatidylinositol 3-kinases (métabolisme), Protein kinases (génétique), Protein kinases (métabolisme), Protein-Serine-Threonine Kinases (génétique), Protein-Serine-Threonine Kinases (métabolisme), Protéines G rho (génétique), Protéines G rho (métabolisme), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines du cycle cellulaire (génétique), Protéines du cycle cellulaire (métabolisme), Protéines et peptides de signalisation intracellulaire (génétique), Protéines et peptides de signalisation intracellulaire (métabolisme), Saccharomyces cerevisiae (croissance et développement), Saccharomyces cerevisiae (enzymologie), Saccharomyces cerevisiae (génétique), Transduction du signal (physiologie).
MESH :
- croissance et développement : Saccharomyces cerevisiae.
- enzymologie : Saccharomyces cerevisiae.
- génétique : Activation enzymatique, Facteurs d'échange de nucléotides guanyliques, Glucose, Phosphatidylinositol 3-kinases, Protein kinases, Protein-Serine-Threonine Kinases, Protéines G rho, Protéines de Saccharomyces cerevisiae, Protéines du cycle cellulaire, Protéines et peptides de signalisation intracellulaire, Saccharomyces cerevisiae.
- métabolisme : Facteurs d'échange de nucléotides guanyliques, Glucose, Phosphatidylinositol 3-kinases, Protein kinases, Protein-Serine-Threonine Kinases, Protéines G rho, Protéines de Saccharomyces cerevisiae, Protéines du cycle cellulaire, Protéines et peptides de signalisation intracellulaire.
- physiologie : Transduction du signal.
- Mutation.

English descriptors

Abstract

In Saccharomyces cerevisiae, phosphorylation of Ugp1 by either of the yeast PASK family protein kinases (yPASK), Psk1 or Psk2, directs this metabolic enzyme to deliver glucose to the periphery for synthesis of the cell wall. However, we isolated PSK1 and PSK2 in a high-copy suppressor screen of a temperature-sensitive mutant of target of rapamycin 2 (TOR2). Posttranslational activation of yPASK, either by cell integrity stress or by growth on nonfermentative carbon sources, also suppressed the growth defect resulting from tor2 mutation. Although suppression of the tor2 mutant growth phenotype by activation of the kinase activity of yPASK required phosphorylation of the metabolic enzyme Ugp1 on serine 11, this resulted in the formation of a complex that induced Rho1 activation, rather than required the glucose partitioning function of Ugp1. In addition to phosphorylated Ugp1, this complex contained Rom2, a Rho1 guanine nucleotide exchange factor, and Ssd1, an mRNA-binding protein. Activation of yPASK-dependent Ugp1 phosphorylation, therefore, enables two processes that are required for cell growth and stress resistance: synthesis of the cell wall through partitioning glucose to the periphery and the formation of the signaling complex with Rom2 and Ssd1 to promote Rho1-dependent polarized cell growth. This complex may integrate metabolic and signaling responses required for cell growth and survival in suboptimal conditions.

DOI: 10.1126/scisignal.2002435
PubMed: 22296835
PubMed Central: PMC3930472

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<front><div type="abstract" xml:lang="en">In Saccharomyces cerevisiae, phosphorylation of Ugp1 by either of the yeast PASK family protein kinases (yPASK), Psk1 or Psk2, directs this metabolic enzyme to deliver glucose to the periphery for synthesis of the cell wall. However, we isolated PSK1 and PSK2 in a high-copy suppressor screen of a temperature-sensitive mutant of target of rapamycin 2 (TOR2). Posttranslational activation of yPASK, either by cell integrity stress or by growth on nonfermentative carbon sources, also suppressed the growth defect resulting from tor2 mutation. Although suppression of the tor2 mutant growth phenotype by activation of the kinase activity of yPASK required phosphorylation of the metabolic enzyme Ugp1 on serine 11, this resulted in the formation of a complex that induced Rho1 activation, rather than required the glucose partitioning function of Ugp1. In addition to phosphorylated Ugp1, this complex contained Rom2, a Rho1 guanine nucleotide exchange factor, and Ssd1, an mRNA-binding protein. Activation of yPASK-dependent Ugp1 phosphorylation, therefore, enables two processes that are required for cell growth and stress resistance: synthesis of the cell wall through partitioning glucose to the periphery and the formation of the signaling complex with Rom2 and Ssd1 to promote Rho1-dependent polarized cell growth. This complex may integrate metabolic and signaling responses required for cell growth and survival in suboptimal conditions.</div>
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PAS kinase promotes cell survival and growth through activation of Rho1.

PAS kinase promotes cell survival and growth through activation of Rho1.

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