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Post-translational modifications regulate signalling by Ror1

Basic information
Original title:Post-translational modifications regulate signalling by Ror1
Authors:Markéta Kaucká, Pavel Krejčí, Karla Plevová, Šárka Pavlová, Jiřina Procházková, Pavlína Janovská, Jana Valnohová, Alois Kozubík, Šárka Pospíšilová, Vítězslav Bryja
Further information
Citation:KAUCKÁ, Markéta, Pavel KREJČÍ, Karla PLEVOVÁ, Šárka PAVLOVÁ, Jiřina PROCHÁZKOVÁ, Pavlína JANOVSKÁ, Jana VALNOHOVÁ, Alois KOZUBÍK, Šárka POSPÍŠILOVÁ and Vítězslav BRYJA. Post-translational modifications regulate signalling by Ror1 (Post-translational modifications regulate signalling by Ror1). Acta Physiologica, Oxford: Blackwell Publishing, 2011, vol. 203, No 3, p. 351-362. ISSN 1748-1708. doi:10.1111/j.1748-1716.2011.02306.x.Export BibTeX
@article{961182,
author = {Kaucká, Markéta and Krejčí, Pavel and Plevová, Karla and Pavlová, Šárka and Procházková, Jiřina and Janovská, Pavlína and Valnohová, Jana and Kozubík, Alois and Pospíšilová, Šárka and Bryja, Vítězslav},
article_location = {Oxford},
article_number = {3},
doi = {http://dx.doi.org/10.1111/j.1748-1716.2011.02306.x},
keywords = {Ror1; posttranslational modifications; glycosylation; chronic lymphocytic leukemia},
language = {eng},
issn = {1748-1708},
journal = {Acta Physiologica},
title = {Post-translational modifications regulate signalling by Ror1},
volume = {203},
year = {2011}
}
Original language:English
Field:Genetics and molecular biology
Type:Article in Periodical
Keywords:Ror1; posttranslational modifications; glycosylation; chronic lymphocytic leukemia

Ror1 (receptor tyrosine kinase-like orphan receptor)is highly upregulated in B cells of patients with chronic lymphocytic leukaemia (CLL). Ror1 acts as the Wnt receptor in the non-canonical Wnt pathway. 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. Moreover, we show that 130-kDa Ror1 is mono-ubiquitinated. Furthermore, individual CLL patients show striking differences in the electrophoretic migration of Ror1, which correspond to the level of glycosylation. Our data show that Ror1 undergoes complex post-translational modifications by glycosylation and mono-ubiquitination. These modifications regulate Ror1 localization and signalling, and are highly variable among individual CLL patients. These may suggest that Ror1 signals only in a subset of CLL patients despite Ror1 levels are ubiquitously high in all CLL patients.

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