Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1999-10-21
pubmed:abstractText
The cAMP-protein kinase A (PKA) pathway in the yeast Saccharomyces cerevisiae plays a major role in the control of metabolism, stress resistance and proliferation, in particular in connection with the available nutrient conditions. Extensive information has been obtained on the core section of the pathway, i.e. Cdc25, Ras, adenylate cyclase, PKA, and on components interacting directly with this core section, such as the Ira proteins, Cap/Srv2 and the two cAMP phosphodiesterases. Recent work has now started to reveal upstream regulatory components and downstream targets of the pathway. A G-protein-coupled receptor system (Gpr1-Gpa2) acts upstream of adenylate cyclase and is required for glucose activation of cAMP synthesis in concert with a glucose phosphorylation-dependent mechanism. Although a genuine signalling role for the Ras proteins remains unclear, they appear to mediate at least part of the potent stimulation of cAMP synthesis by intracellular acidification. Recently, several new targets of the PKA pathway have been discovered. These include the Msn2 and Msn4 transcription factors mediating part of the induction of STRE-controlled genes by a variety of stress conditions, the Rim15 protein kinase involved in stationary phase induction of a similar set of genes and the Pde1 low-affinity cAMP phosphodiesterase, which specifically controls agonist-induced cAMP signalling. A major issue that remains to be resolved is the precise connection between the cAMP-PKA pathway and other nutrient-regulated components involved in the control of growth and of phenotypic characteristics correlated with growth, such as the Sch9 and Yak1 protein kinases. Cln3 appears to play a crucial role in the connection between the availability of certain nutrients and Cdc28 kinase activity, but it remains to be clarified which nutrient-controlled pathways control Cln3 levels.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/3',5'-Cyclic-AMP Phosphodiesterases, http://linkedlifedata.com/resource/pubmed/chemical/3',5'-Cyclic-GMP Phosphodiesterases, http://linkedlifedata.com/resource/pubmed/chemical/Adenylate Cyclase, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic Nucleotide..., http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/GPR1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Protein alpha Subunits, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Glucose, http://linkedlifedata.com/resource/pubmed/chemical/Gpa2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Heterotrimeric GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Diester Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, G-Protein-Coupled, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/ras Proteins
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0950-382X
pubmed:author
pubmed:issnType
Print
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
904-18
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10476026-3',5'-Cyclic-AMP Phosphodiesterases, pubmed-meshheading:10476026-3',5'-Cyclic-GMP Phosphodiesterases, pubmed-meshheading:10476026-Adenylate Cyclase, pubmed-meshheading:10476026-Cyclic AMP, pubmed-meshheading:10476026-Cyclic AMP-Dependent Protein Kinases, pubmed-meshheading:10476026-Cyclic Nucleotide Phosphodiesterases, Type 1, pubmed-meshheading:10476026-Fungal Proteins, pubmed-meshheading:10476026-GTP-Binding Protein alpha Subunits, pubmed-meshheading:10476026-GTP-Binding Proteins, pubmed-meshheading:10476026-Glucose, pubmed-meshheading:10476026-Heterotrimeric GTP-Binding Proteins, pubmed-meshheading:10476026-Molecular Sequence Data, pubmed-meshheading:10476026-Phosphoric Diester Hydrolases, pubmed-meshheading:10476026-Receptors, Cell Surface, pubmed-meshheading:10476026-Receptors, G-Protein-Coupled, pubmed-meshheading:10476026-Saccharomyces cerevisiae, pubmed-meshheading:10476026-Saccharomyces cerevisiae Proteins, pubmed-meshheading:10476026-Signal Transduction, pubmed-meshheading:10476026-Transcription, Genetic, pubmed-meshheading:10476026-ras Proteins
pubmed:year
1999
pubmed:articleTitle
Novel sensing mechanisms and targets for the cAMP-protein kinase A pathway in the yeast Saccharomyces cerevisiae.
pubmed:affiliation
Laboratorium voor Moleculaire Celbiologie, Katholieke Universiteit Leuven, Kardinaal Mercierlaan 92, B-3001 Leuven-Heverlee, Flanders, Belgium. johan.thevelein@bio.kuleuven.ac.be
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't