Detailed Information on Publication Record
2011
Post-translational modifications regulate signalling by Ror1
KAUCKÁ, Markéta, Pavel KREJČÍ, Karla PLEVOVÁ, Šárka PAVLOVÁ, Jiřina PROCHÁZKOVÁ et. al.Basic information
Original name
Post-translational modifications regulate signalling by Ror1
Authors
KAUCKÁ, Markéta (203 Czech Republic, belonging to the institution), Pavel KREJČÍ (203 Czech Republic, belonging to the institution), Karla PLEVOVÁ (203 Czech Republic, belonging to the institution), Šárka PAVLOVÁ (203 Czech Republic, belonging to the institution), Jiřina PROCHÁZKOVÁ (203 Czech Republic, belonging to the institution), Pavlína JANOVSKÁ (203 Czech Republic, belonging to the institution), Jana VALNOHOVÁ (203 Czech Republic, belonging to the institution), Alois KOZUBÍK (203 Czech Republic, belonging to the institution), Šárka POSPÍŠILOVÁ (203 Czech Republic, belonging to the institution) and Vítězslav BRYJA (203 Czech Republic, guarantor)
Edition
Acta Physiologica, Oxford, Blackwell Publishing, 2011, 1748-1708
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
Genetics and molecular biology
Country of publisher
United Kingdom of Great Britain and Northern Ireland
Confidentiality degree
není předmětem státního či obchodního tajemství
Impact factor
Impact factor: 3.090
RIV identification code
RIV/00216224:14310/11:00050218
Organization unit
Faculty of Science
UT WoS
000296061800002
Keywords in English
Ror1; posttranslational modifications; glycosylation; chronic lymphocytic leukemia
Změněno: 20/4/2012 11:39, Ing. Andrea Mikešková
Abstract
V originále
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.
Links
GAP301/11/0747, research and development project |
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GAP305/11/0752, research and development project |
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GA301/09/0587, research and development project |
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GD204/09/H058, research and development project |
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MSM0021622430, plan (intention) |
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MUNI/E/0128/2009, interní kód MU |
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NT11217-5/2010, interní kód MU |
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1658, interní kód MU |
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