Linked Life Data

20054684

Source:http://linkedlifedata.com/resource/pubmed/id/20054684

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2010-2-24
pubmed:abstractText
The double disruptant of the S. cerevisiae protein phosphatase (PPase) genes, PTP2 (phosphotyrosine-specific PPase) and MSG5 (phosphotyrosine and phosphothreonine/serine-PPase) causes calcium-sensitive growth (Cas). Previous study using Fluorescent-activated cell sorting (FACS) analysis showed that this growth defect with calcium occurs at G1-S transition in the cell cycle. We discovered that six non-essential protein kinase (PKase) disruptions (Deltabck1, Deltamkk1, Deltaslt2/Deltampk1, Deltamck1, Deltassk2 and Deltayak1) suppressed the Cas-phenotype of the Deltaptp2 Deltamsg5 double disruptant. Bck1p, Mkk1p and Slt2p are components of the mitogen-activated protein kinase (MAPK) cascade of cell wall integrity pathway (Slt2 pathway), and Mck1p is its down regulator. Ssk2p is the MAPK kinase kinase of the high-osmolarity glycerol (HOG) pathway, while Yak1p is a negative regulator for the cAMP-dependent PKA pathway. FACS analysis revealed that only the disruption of Deltassk2 and Deltayak1 but not Deltabck1, Deltamkk1, Deltaslt2 and Deltamck1 was able to suppress the delayed G1-S transition, suggesting that suppression of the growth defect is not always accompanied by suppression of the G1-S transition delay. The discovery of these PKases as suppressors revealed that in addition to the previously anticipated Slt2 pathway, HOG, Yak1p and Mck1p regulatory pathways may also be involved in the calcium sensitivity of the Deltaptp2 Deltamsg5 double disruptant.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Calcium, http://linkedlifedata.com/resource/pubmed/chemical/HOG1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides..., http://linkedlifedata.com/resource/pubmed/chemical/MAP Kinase Kinase Kinases, http://linkedlifedata.com/resource/pubmed/chemical/MSG5 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Ptp2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/SLT2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/SSK2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/YAK1 protein, S cerevisiae
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1432-072X
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
192
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
157-65
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Identification of protein kinase disruptions as suppressors of the calcium sensitivity of S. cerevisiae Deltaptp2 Deltamsg5 protein phosphatase double disruptant.
pubmed:affiliation
Department of Biotechnology, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't