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The cytoplasmic domain of chondrolectin interacts with the β-subunit of rab geranylgeranyl transferase
1University of Antwerp
© 2007 Versita Warsaw. This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License. (CC BY-NC-ND 3.0)
Citation Information: Cellular and Molecular Biology Letters. Volume 13, Issue 2, Pages 250–259, ISSN (Online) 1689-1392, DOI: 10.2478/s11658-007-0052-8, April 2008
- Published Online:
Mouse chondrolectin (chodl) was isolated out of the tail tip of four-day old 129/SvJ mice as a by-product of a PCR-based subtractive cDNA library screening. The gene is predominantly expressed in adult skeletal muscle, heart, testes and lungs and in embryonic stadia. Chodl is the mouse homologue of human chondrolectin (CHODL), a gene that encodes for a type Ia transmembrane protein and that is expressed in human testis, prostate, heart and skeletal muscle tissue. CHODL-splice variants (CHODL f, CHODL fΔE, CHODL ΔE) are detected in human leukocytes. The proteins of the chondrolectin family belong to the family of C-type lectins. As the members of this protein family are important for a wide array of biological processes, the function of chodl was investigated by searching for its protein interaction partners. The β-subunit of Rab geranylgeranyl transferase (Rabggtb) was isolated 8 times after a complete Sos recruitment system (SRS) screen with the cytoplasmic domain of chodl. The interaction was confirmed with in vitro transcription/translation and co-immunoprecipitation (co-IP) experiments.