Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1998-12-30
pubmed:abstractText
The Saccharomyces cerevisiae PLC1 gene encodes a homolog of the delta isoform of mammalian phosphoinositide-specific phospholipase C. Cells deleted for PLC1 gene (plc1Delta) are viable but display several phenotypes, including temperature and osmotic sensitivity and defects in utilization of carbon sources other than glucose. We have used the two hybrid screen to identify Plc1p-interacting proteins. One of the identified proteins was Tor2p, a putative phosphatidylinositol (PtdIns) kinase involved in regulation of protein synthesis, cell cycle progression and organization of the actin cytoskeleton. This interaction was confirmed biochemically by coprecipitation of Plc1p and Tor2p. The results suggest that Tor2p, as a PtdIns kinase, produces phosphorylated PtdIns, which is then hydrolyzed by the associated Plc1p. The proximity of Tor2p to Plc1p may therefore result in a regulated spatial and temporal coupling of synthesis and hydrolysis of phosphorylated forms of PtdIns.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 1998 Academic Press.
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
252
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
285-9
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Phosphoinositide-specific phospholipase C interacts with phosphatidylinositol kinase homolog TOR2.
pubmed:affiliation
Department of Biological Sciences, St. John's University, Jamaica, New York, 11439, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't