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We report here the presence of a potent 3\u2010phosphatase activity in different cell types. This activity is detected both in cytosol and membranes of A431 cells and is inhibited by VO<jats:sub>4<\/jats:sub>\n<jats:sup>3\u2212<\/jats:sup> and Zn<jats:sup>2+<\/jats:sup>. Interestingly, the cytosolic activity from A431 cells selectively hydrolyzes in vitro PtdIns(3)P and PtdIns(3,4)P<jats:sub>2<\/jats:sub>, whereas PtdIns(3,4,5)P<jats:sub>3<\/jats:sub> remains a very poor substrate under the same conditions. Finally, assays of phosphatidylinositol 3\u2010kinase and 3\u2010phosphatase activities in the pool of phosphotyrosine\u2010containing proteins isolated from EGF\u2010stimulated A431 cells suggest a compartmentation of these two antagonistic activities during cell activation.<\/jats:p>","DOI":"10.1016\/0014-5793(94)80251-3","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T09:09:11Z","timestamp":1027588151000},"page":"113-118","source":"Crossref","is-referenced-by-count":12,"title":["Phosphoinositide 3\u2010phosphatase segregates from phosphatidylinositol 3\u2010kinase in EGF\u2010stimulated A431 cells and fails to in vitro hydrolyse 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