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Despite this, the site and nature of this membrane association has not been fully characterised\u00a0upon platelet activation. High resolution imaging showed that cPLA<jats:sub>2<\/jats:sub>\u03b1 was distributed in a partly structured manner throughout the resting platelet. Upon glass activation or thrombin stimulation, cPLA<jats:sub>2<\/jats:sub>\u03b1 relocated to a peripheral region corresponding to the platelet plasma membrane. Upon thrombin stimulation of platelets a major pool of cPLA<jats:sub>2<\/jats:sub>\u03b1 was associated with the plasma membrane in an EGTA\u2010resistant manner. EGTA\u2010resistant membrane binding was abolished upon de\u2010polymerisation of actin filaments by DNase I and furthermore, cPLA<jats:sub>2<\/jats:sub>\u03b1 co\u2010immunoprecipitated with actin upon thrombin stimulation of platelets. Immunofluorescence microscopy studies revealed that, upon platelet activation, cPLA<jats:sub>2<\/jats:sub>\u03b1 and actin co\u2010localised at the plasma membrane. Thus we have identified a novel mechanism for the interaction of cPLA<jats:sub>2<\/jats:sub>\u03b1 with its membrane substrate via interaction with actin.<\/jats:p>","DOI":"10.1016\/j.cellbi.2008.09.010","type":"journal-article","created":{"date-parts":[[2008,10,8]],"date-time":"2008-10-08T19:03:32Z","timestamp":1223492612000},"page":"83-91","update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Association with actin mediates the EGTA\u2010resistant binding of cytosolic phospholipase A<sub>2<\/sub>\u2010\u03b1 to the plasma membrane of activated platelets"],"prefix":"10.1002","volume":"33","author":[{"given":"Ann D.","family":"Hastings","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shane 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