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The ubiquitin C-terminal hydrolase UCH-L1 regulates B-cell proliferation and integrin activation
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2009 (English)In: Journal of Cellular and Molecular Medicine (Print), ISSN 1582-1838, E-ISSN 1582-4934, Vol. 13, no 8b, p. 1666-1678Article in journal (Refereed) Published
Abstract [en]

The ubiquitin C-terminal hydrolase-L1 (UCH-L1) is a deubiquitinating enzyme that catalyses the hydrolysis of polyubiquitin precursors and small ubiquitin adducts. UCH-L1 has been detected in a variety of malignant and metastatic tumours but its biological function in these cells is unknown. We have previously shown that UCH-L1 is highly expressed in Burkitt's lymphoma (BL) and is up-regulated upon infection of B lymphocytes with Epstein-Barr virus (EBV). Here we show that knockdown of UCH-L1 by RNAi inhibits the proliferation of BL cells in suspension and semisolid agar and activates strong LFA-1-dependent homotypic adhesion. Induction of cell adhesion correlated with cation-induced binding to ICAM-1, clustering of LFA-1 into lipid rafts and constitutive activation of the Rap1 and Rac1 GTPases. Expression of a catalytically active UCH-L1 promoted the proliferation of a UCH-L1-negative EBV transformed lymphoblastoid cell line (LCL) and inhibited cell adhesion, whereas a catalytic mutant had no effect, confirming the requirement of UCH-L1 enzymatic activity for the regulation of these phenotypes. Our results identify UCH-L1 as a new player in the signalling pathways that promote the proliferation and invasive capacity of malignant B cells.

Place, publisher, year, edition, pages
John Wiley & Sons, 2009. Vol. 13, no 8b, p. 1666-1678
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Cell and Molecular Biology Immunology Microbiology
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URN: urn:nbn:se:umu:diva-165150DOI: 10.1111/j.1582-4934.2008.00501.xISI: 000272190800006PubMedID: 20187292OAI: oai:DiVA.org:umu-165150DiVA, id: diva2:1369416
Available from: 2019-11-12 Created: 2019-11-12 Last updated: 2019-11-12Bibliographically approved

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Frisan, Teresa

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