Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5460
pubmed:dateCreated
2000-4-4
pubmed:abstractText
Phospholipase C and two inositol polyphosphate (IP) kinases constitute a signaling pathway that regulates nuclear messenger RNA export through production of inositol hexakisphosphate (IP6). The inositol 1,4,5-trisphosphate kinase of this pathway in Saccharomyces cerevisiae, designated Ipk2, was found to be identical to Arg82, a regulator of the transcriptional complex ArgR-Mcm1. Synthesis of inositol 1,4,5,6-tetrakisphosphate, but not IP6, was required for gene regulation through ArgR-Mcm1. Thus, the phospholipase C pathway produces multiple IP messengers that modulate distinct nuclear processes. The results reveal a direct mechanism by which activation of IP signaling may control gene expression.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Arginine, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Inositol 1,4,5-Trisphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Inositol 1,4,5-trisphosphate..., http://linkedlifedata.com/resource/pubmed/chemical/Inositol Phosphates, http://linkedlifedata.com/resource/pubmed/chemical/MCM1 Protein, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Alcohol Group..., http://linkedlifedata.com/resource/pubmed/chemical/Phytic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases, http://linkedlifedata.com/resource/pubmed/chemical/inositol..., http://linkedlifedata.com/resource/pubmed/chemical/inositol-1,4,5,6-tetrakisphosphate
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
287
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2026-9
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:10720331-Amino Acid Sequence, pubmed-meshheading:10720331-Arginine, pubmed-meshheading:10720331-Cell Nucleus, pubmed-meshheading:10720331-DNA-Binding Proteins, pubmed-meshheading:10720331-Gene Expression Regulation, Fungal, pubmed-meshheading:10720331-Inositol 1,4,5-Trisphosphate, pubmed-meshheading:10720331-Inositol Phosphates, pubmed-meshheading:10720331-MCM1 Protein, pubmed-meshheading:10720331-Molecular Sequence Data, pubmed-meshheading:10720331-Phosphoric Monoester Hydrolases, pubmed-meshheading:10720331-Phosphorylation, pubmed-meshheading:10720331-Phosphotransferases (Alcohol Group Acceptor), pubmed-meshheading:10720331-Phytic Acid, pubmed-meshheading:10720331-Saccharomyces cerevisiae, pubmed-meshheading:10720331-Signal Transduction, pubmed-meshheading:10720331-Transcription, Genetic, pubmed-meshheading:10720331-Transcription Factors, pubmed-meshheading:10720331-Type C Phospholipases
pubmed:year
2000
pubmed:articleTitle
A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional control.
pubmed:affiliation
Departments of Pharmacology and Cancer Biology and of Biochemistry, Duke University Medical Center, DUMC 3813, Durham, NC 27710, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't