| pubmed-article:11311145 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11311145 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:11311145 | lifeskim:mentions | umls-concept:C0024660 | lld:lifeskim |
| pubmed-article:11311145 | lifeskim:mentions | umls-concept:C0332197 | lld:lifeskim |
| pubmed-article:11311145 | lifeskim:mentions | umls-concept:C0063593 | lld:lifeskim |
| pubmed-article:11311145 | lifeskim:mentions | umls-concept:C1418557 | lld:lifeskim |
| pubmed-article:11311145 | pubmed:issue | Pt 3 | lld:pubmed |
| pubmed-article:11311145 | pubmed:dateCreated | 2001-4-20 | lld:pubmed |
| pubmed-article:11311145 | pubmed:abstractText | Phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P(2)] plays a complex role in generating intracellular signalling molecules, and also in regulating actin-binding proteins, vesicular trafficking and vacuolar fusion. Four inositol polyphosphate 5-phosphatases (hereafter called 5-phosphatases) have been identified in Saccharomyces cerevisiae: Inp51p, Inp52p, Inp53p and Inp54p. Each enzyme contains a 5-phosphatase domain which hydrolyses PtdIns(4,5)P(2), forming PtdIns4P, while Inp52p and Inp53p also express a polyphosphoinositide phosphatase domain within the Sac1-like domain. Disruption of any two yeast 5-phosphatases containing a Sac1-like domain results in abnormalities in actin polymerization, plasma membrane, vacuolar morphology and bud-site selection. Triple null mutant 5-phosphatase strains are non-viable. To investigate the role of PtdIns(4,5)P(2) in mediating the phenotype of double and triple 5-phosphatase null mutant yeast, we determined whether a mammalian PtdIns(4,5)P(2) 5-phosphatase, 5-phosphatase II, which lacks polyphosphoinositide phosphatase activity, could correct the phenotype of triple 5-phosphatase null mutant yeast and restore cellular PtdIns(4,5)P(2) levels to near basal values. Mammalian 5-phosphatase II expressed under an inducible promoter corrected the growth, cell wall, vacuolar and actin polymerization defects of the triple 5-phosphatase null mutant yeast strains. Cellular PtdIns(4,5)P(2) levels in various 5-phosphatase double null mutant strains demonstrated significant accumulation (4.5-, 3- and 2-fold for Deltainp51Deltainp53, Deltainp51Deltainp52 and Deltainp52Deltainp53 double null mutants respectively), which was corrected significantly following 5-phosphatase II expression. Collectively, these studies demonstrate the functional and cellular consequences of PtdIns(4,5)P(2) accumulation and the evolutionary conservation of function between mammalian and yeast PtdIns(4,5)P(2) 5-phosphatases. | lld:pubmed |
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| pubmed-article:11311145 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11311145 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11311145 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11311145 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11311145 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11311145 | pubmed:month | May | lld:pubmed |
| pubmed-article:11311145 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:11311145 | pubmed:author | pubmed-author:MitchellC ACA | lld:pubmed |
| pubmed-article:11311145 | pubmed:author | pubmed-author:SambrookJJ | lld:pubmed |
| pubmed-article:11311145 | pubmed:author | pubmed-author:O'MalleyC JCJ | lld:pubmed |
| pubmed-article:11311145 | pubmed:author | pubmed-author:EllisS LSL | lld:pubmed |
| pubmed-article:11311145 | pubmed:author | pubmed-author:KongA MAM | lld:pubmed |
| pubmed-article:11311145 | pubmed:author | pubmed-author:McCollB KBK | lld:pubmed |
| pubmed-article:11311145 | pubmed:author | pubmed-author:WijayaratnamA... | lld:pubmed |
| pubmed-article:11311145 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11311145 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:11311145 | pubmed:volume | 355 | lld:pubmed |
| pubmed-article:11311145 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11311145 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11311145 | pubmed:pagination | 805-17 | lld:pubmed |
| pubmed-article:11311145 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:11311145 | pubmed:meshHeading | pubmed-meshheading:11311145... | lld:pubmed |
| pubmed-article:11311145 | pubmed:meshHeading | pubmed-meshheading:11311145... | lld:pubmed |
| pubmed-article:11311145 | pubmed:meshHeading | pubmed-meshheading:11311145... | lld:pubmed |
| pubmed-article:11311145 | pubmed:meshHeading | pubmed-meshheading:11311145... | lld:pubmed |
| pubmed-article:11311145 | pubmed:meshHeading | pubmed-meshheading:11311145... | lld:pubmed |
| pubmed-article:11311145 | pubmed:meshHeading | pubmed-meshheading:11311145... | lld:pubmed |
| pubmed-article:11311145 | pubmed:meshHeading | pubmed-meshheading:11311145... | lld:pubmed |
| pubmed-article:11311145 | pubmed:meshHeading | pubmed-meshheading:11311145... | lld:pubmed |
| pubmed-article:11311145 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11311145 | pubmed:articleTitle | Mammalian inositol polyphosphate 5-phosphatase II can compensate for the absence of all three yeast Sac1-like-domain-containing 5-phosphatases. | lld:pubmed |
| pubmed-article:11311145 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, Monash University, Melbourne, Victoria 3800, Australia. cindy.omalley@bbsrc.ac.uk | lld:pubmed |
| pubmed-article:11311145 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11311145 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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