0440915 - BFÚ 2015 RIV US eng J - Článek v odborném periodiku
Kaucká, M. - Krejčí, Pavel - Plevová, K. - Pavlová, Š. - Procházková, Jiřina - Janovská, P. - Valnohová, J. - Kozubík, Alois - Pospíšilová, Š. - Bryja, Vítězslav
Post-translational modifications regulate signalling by Ror1.
Acta Physiologica. Roč. 203, č. 3 (2011), s. 351-362. ISSN 1748-1708. E-ISSN 1748-1716
Institucionální podpora: RVO:68081707
Klíčová slova: chronic lymphocytic leukaemia * glycosylation * post-translational modification
Kód oboru RIV: BO - Biofyzika
Impakt faktor: 3.090, rok: 2011 ; AIS: 1.058, rok: 2011
DOI: https://doi.org/10.1111/j.1748-1716.2011.02306.x

Aim: In this study, we analysed the post-translational modification of receptor tyrosine kinase-like orphan receptor (Ror1). Ror1 is highly upregulated in B cells of patients with chronic lymphocytic leukaemia (CLL). Molecularly, Ror1 acts as the Wnt receptor in the non-canonical Wnt pathway. Methods: The level of Ror1 glycosylation in HEK293 cells and in primary human CLL cells was analysed by treatment of inhibitors interfering with different steps of glycosylation process and by direct treatment of cell lysates with N-glycosidase. Ror1 ubiquitination was determined by ubiquitination assay. Functional consequences of post-translational modifications were analysed by immunohistochemistry and by analysis of cell surface proteins. Differences in Ror1 glycosylation were confirmed by analysis of 14 samples of B cells from CLL patients. Results: We demonstrate that Ror1 is extensively modified by N-linked glycosylation. Glycosylation produces several variants of Ror1 with electrophoretic migration of approx. 100, 115 and 130 kDa. Inhibition of glycosylation interferes with cell surface localization of the 130-kDa variant of Ror1 and prevents Ror1-induced formation of filopodia.
Trvalý link: http://hdl.handle.net/11104/0244017