18059263

Source:http://linkedlifedata.com/resource/pubmed/id/18059263

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0021547, umls-concept:C0034320, umls-concept:C0851285, umls-concept:C1167622, umls-concept:C1853126
pubmed:issue	1
pubmed:dateCreated	2007-12-17
pubmed:databankReference	http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/26740886, http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/26740887, http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/26740888, http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/26740889, http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/26740890, http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/26740891
pubmed:abstractText	When Saccharomyces cerevisiae cells are starved of inorganic phosphate, the Pho80-Pho85 cyclin-cyclin-dependent kinase (CDK) is inactivated by the Pho81 CDK inhibitor (CKI). The regulation of Pho80-Pho85 is distinct from previously characterized mechanisms of CDK regulation: the Pho81 CKI is constitutively associated with Pho80-Pho85, and a small-molecule ligand, inositol heptakisphosphate (IP7), is required for kinase inactivation. We investigated the molecular basis of the IP7- and Pho81-dependent Pho80-Pho85 inactivation using electrophoretic mobility shift assays, enzyme kinetics and fluorescence spectroscopy. We found that IP7 interacts noncovalently with Pho80-Pho85-Pho81 and induces additional interactions between Pho81 and Pho80-Pho85 that prevent substrates from accessing the kinase active site. Using synthetic peptides corresponding to Pho81, we define regions of Pho81 responsible for constitutive Pho80-Pho85 binding and IP7-regulated interaction and inhibition. These findings expand our understanding of the mechanisms of cyclin-CDK regulation and of the biochemical mechanisms of IP7 action.
pubmed:grant	http://linkedlifedata.com/resource/pubmed/grant/R01 GM051377, http://linkedlifedata.com/resource/pubmed/grant/R01 GM051377-15
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pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/101231976
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Cyclins, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Inositol Phosphates, http://linkedlifedata.com/resource/pubmed/chemical/PHO4 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/PHO80 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/PHO81 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/PHO85 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/inositol heptakisphosphate
pubmed:status	MEDLINE
pubmed:month	Jan
pubmed:issn	1552-4469
pubmed:author	pubmed-author:HuangKexinK, pubmed-author:LeeYoung-SamYS, pubmed-author:O'SheaErin KEK, pubmed-author:QuiochoFlorante AFA
pubmed:issnType	Electronic
pubmed:volume	4
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	25-32
pubmed:dateRevised	2011-9-26
pubmed:meshHeading	pubmed-meshheading:18059263-Cyclin-Dependent Kinases, pubmed-meshheading:18059263-Cyclins, pubmed-meshheading:18059263-DNA-Binding Proteins, pubmed-meshheading:18059263-Electrophoretic Mobility Shift Assay, pubmed-meshheading:18059263-Inositol Phosphates, pubmed-meshheading:18059263-Protein Binding, pubmed-meshheading:18059263-Recombinant Proteins, pubmed-meshheading:18059263-Repressor Proteins, pubmed-meshheading:18059263-Saccharomyces cerevisiae, pubmed-meshheading:18059263-Saccharomyces cerevisiae Proteins, pubmed-meshheading:18059263-Substrate Specificity, pubmed-meshheading:18059263-Transcription Factors
pubmed:year	2008
pubmed:articleTitle	Molecular basis of cyclin-CDK-CKI regulation by reversible binding of an inositol pyrophosphate.
pubmed:affiliation	Howard Hughes Medical Institute, Harvard University, Department of Molecular and Cellular Biology, Faculty of Arts and Sciences Center for Systems Biology, 7 Divinity Avenue, Cambridge, Massachusetts 02138, USA.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural