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We have previously shown that UCH\u2010L1 is highly expressed in Burkitt\u2019s lymphoma (BL) and is up\u2010regulated upon infection of B lymphocytes with Epstein\u2013Barr virus (EBV). Here we show that knockdown of UCH\u2010L1 by RNAi inhibits the proliferation of BL cells in suspension and semisolid agar and activates strong LFA\u20101\u2010dependent homotypic adhesion. Induction of cell adhesion correlated with cation\u2010induced binding to ICAM\u20101, clustering of LFA\u20101 into lipid rafts and constitutive activation of the Rap1 and Rac1 GTPases. Expression of a catalytically active UCH\u2010L1 promoted the proliferation of a UCH\u2010L1\u2010negative EBV transformed lymphoblastoid cell line (LCL) and inhibited cell adhesion, whereas a catalytic mutant had no effect, confirming the requirement of UCH\u2010L1 enzymatic activity for the regulation of these phenotypes. Our results identify UCH\u2010L1 as a new player in the signalling pathways that promote the proliferation and invasive capacity of malignant B cells.<\/jats:p>","DOI":"10.1111\/j.1582-4934.2008.00501.x","type":"journal-article","created":{"date-parts":[[2008,9,16]],"date-time":"2008-09-16T16:25:49Z","timestamp":1221582349000},"page":"1666-1678","source":"Crossref","is-referenced-by-count":18,"title":["The ubiquitin C\u2010terminal hydrolase UCH\u2010L1 regulates B\u2010cell proliferation and integrin 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