Title
The cytoplasmic domain of chondrolectin interacts with the <tex>$\beta$</tex>-subunit of rab geranylgeranyl transferase The cytoplasmic domain of chondrolectin interacts with the <tex>$\beta$</tex>-subunit of rab geranylgeranyl transferase
Author
Faculty/Department
Faculty of Pharmaceutical, Biomedical and Veterinary Sciences . Biomedical Sciences
Publication type
article
Publication
Subject
Chemistry
Biology
Human medicine
Source (journal)
Cellular and molecular biology letters / Polish Society for Cell Biology, Wroclaw, PL. - -
Volume/pages
13(2008) :2 , p. 250-259
ISSN
1425-8153
ISI
000254847700007
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
Affiliation
University of Antwerp
Abstract
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 , CHODL Delta , CHODL Delta ) 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 beta-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.
E-info
https://repository.uantwerpen.be/docman/iruaauth/336740/08e6156.pdf
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