|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0001516,
umls-concept:C0018270,
umls-concept:C0024660,
umls-concept:C0036024,
umls-concept:C0598095,
umls-concept:C1334043,
umls-concept:C1415151,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636
|
|
pubmed:issue |
11
|
|
pubmed:dateCreated |
2007-11-13
|
|
pubmed:abstractText |
Nutrient starvation results in the interaction of Saccharomyces cerevisiae cells with each other and with surfaces. Adhesive growth requires the expression of the FLO11 gene regulated by the Ras/cAMP/cAMP-dependent protein kinase, the Kss1p/MAPK, and the Gcn4p/general amino acid control pathway, respectively. Proteomics two-dimensional DIGE experiments revealed post-transcriptionally regulated proteins in response to amino acid starvation including the ribosomal protein Cpc2p/Asc1p. This putative translational regulator is highly conserved throughout the eukaryotic kingdom and orthologous to mammalian RACK1. Deletion of CPC2/ASC1 abolished amino acid starvation-induced adhesive growth and impaired basal expression of FLO11 and its activation upon starvation in haploid cells. In addition, the diploid Flo11p-dependent pseudohyphal growth during nitrogen limitation was CPC2/ASC1-dependent. A more detailed analysis revealed that a CPC2/ASC1 deletion caused increased sensitivity to cell wall drugs suggesting that the gene is required for general cell wall integrity. Phosphoproteome and Western hybridization data indicate that Cpc2p/Asc1p affected the phosphorylation of the translational initiation factors eIF2 alpha and eIF4A and the ribosome-associated complex RAC. A crucial role of Cpc2p/Asc1p at the ribosomal interface coordinating signal transduction, translation initiation, and transcription factor formation was corroborated.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ASC1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-2,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MUC1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Initiation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteome,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/eIF-4
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Nov
|
|
pubmed:issn |
1535-9476
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
6
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1968-79
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:17704055-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:17704055-Amino Acid Sequence,
pubmed-meshheading:17704055-Amino Acids,
pubmed-meshheading:17704055-Cell Adhesion,
pubmed-meshheading:17704055-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:17704055-Eukaryotic Initiation Factor-2,
pubmed-meshheading:17704055-GTP-Binding Proteins,
pubmed-meshheading:17704055-Gene Deletion,
pubmed-meshheading:17704055-Membrane Glycoproteins,
pubmed-meshheading:17704055-Membrane Proteins,
pubmed-meshheading:17704055-Molecular Sequence Data,
pubmed-meshheading:17704055-Peptide Initiation Factors,
pubmed-meshheading:17704055-Phosphoproteins,
pubmed-meshheading:17704055-Proteome,
pubmed-meshheading:17704055-Proteomics,
pubmed-meshheading:17704055-Saccharomyces cerevisiae,
pubmed-meshheading:17704055-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:17704055-Sex Characteristics
|
|
pubmed:year |
2007
|
|
pubmed:articleTitle |
The Saccharomyces homolog of mammalian RACK1, Cpc2/Asc1p, is required for FLO11-dependent adhesive growth and dimorphism.
|
|
pubmed:affiliation |
Institute of Microbiology and Genetics, Georg August University, D-37077 Göttingen, Germany.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
