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Development and Application of Rapamycin-regulated Tyrosine Phosphatases
Published on: September 6, 2024
Post-translational modifications regulate signalling by Ror1.
M Kaucká1, P Krejčí, K Plevová
1Faculty of Science, Institute of Experimental Biology, Masaryk University, Kotlářská, Brno, Czech Republic.
Acta Physiologica (Oxford, England)
|April 13, 2011
Summary
Receptor tyrosine kinase-like orphan receptor (Ror1) undergoes glycosylation and ubiquitination, affecting its cell surface localization and signaling in chronic lymphocytic leukemia (CLL). These modifications vary significantly between CLL patients.
Area of Science:
- Biochemistry
- Molecular Biology
- Oncology
Background:
- Receptor tyrosine kinase-like orphan receptor (Ror1) is a Wnt pathway receptor.
- Ror1 is highly expressed in B cells from chronic lymphocytic leukemia (CLL) patients.
Purpose of the Study:
- To analyze the post-translational modifications of Ror1.
- To investigate the functional consequences of Ror1 modifications in CLL.
Main Methods:
- Analyzed Ror1 glycosylation using glycosylation inhibitors and N-glycosidase in HEK293 and CLL cells.
- Determined Ror1 ubiquitination via ubiquitination assays.
- Assessed functional impacts through immunohistochemistry and cell surface protein analysis.
Main Results:
- Demonstrated extensive N-linked glycosylation of Ror1, creating ~100, 130-kDa variants.
- Inhibition of glycosylation disrupted cell surface Ror1 localization and filopodia formation.
- Identified mono-ubiquitination of the 130-kDa Ror1 variant and significant glycosylation variability among CLL patients.
Conclusions:
- Ror1 exhibits complex glycosylation and mono-ubiquitination.
- These modifications regulate Ror1 localization and signaling.
- Variability in Ror1 modifications suggests differential signaling in CLL patient subsets.
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