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Phosphorylation was stimulated 3\u20135\u2010fold by Ca<jats:sup>2+<\/jats:sup>, however the <jats:italic>K<\/jats:italic>\n<jats:sub>m<\/jats:sub> was the same (2.5\u03bcM) at high or low Ca<jats:sup>2+<\/jats:sup>. Although the level of free Ca<jats:sup>2+<\/jats:sup> needed for this enhanced phosphorylation was 10<jats:sup>\u22124<\/jats:sup>\u201310<jats:sup>\u22123<\/jats:sup>)<jats:sup>\u22123<\/jats:sup> M, phosphatidylserine shifted the Ca<jats:sup>2+<\/jats:sup> sensitivity to the 10<jats:sup>\u22126<\/jats:sup>\u201310<jats:sup>\u22125<\/jats:sup> M range. Independent evidence suggested that p36 interacts directly with liposomes containing phosphatidylserine. This raises the possibility that p36, like c\u2010kinase, is a Ca<jats:sup>2+<\/jats:sup>\u2010activated, phospholipid\u2010dependent protein.<\/jats:p>","DOI":"10.1016\/0014-5793(85)80047-8","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T07:57:58Z","timestamp":1027583878000},"page":"79-82","source":"Crossref","is-referenced-by-count":92,"title":["Phosphorylation of p36 in vitro with pp60<sup>src<\/sup>"],"prefix":"10.1002","volume":"192","author":[{"given":"John R.","family":"Glenney","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2001,11,12]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(80)90446-8"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(80)90445-6"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1128\/MCB.3.3.340"},{"key":"e_1_2_1_5_1","doi-asserted-by":"crossref","unstructured":"Greenberg M.E. and Edelman G.M. 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