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The cytoplasmic domain of chondrolectin interacts with the β-subunit of rab geranylgeranyl transferase


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.







carbohydrate recognition domain


days post coitum


extracellular matrix


Rab geranylgeranyl transferase β


Sos recruitment system


  1. Weng, L., Hübner, R., Claessens, A., Smits, P., Wauters, J., Tylzanowski, P., Van Marck, E. and Merregaert, J. Isolation and characterization of a novel C-type lectin, Chondrolectin (Chodl), which is predominantly expressed in muscle cells. Gene 308 (2003) 21–29.

    PubMed  Article  CAS  Google Scholar 

  2. Weng, L., Smits, P., Wauters, J. and Merregaert, J. Molecular cloning and characterization of human Chondrolectin, a novel type I transmembrane protein homologous to C-type lectins. Genomics 80 (2002) 62–70.

    PubMed  Article  CAS  Google Scholar 

  3. Claessens, A., Van de Vijver, K., Van Bockstaele, D.R., Wauters, J., Berneman, Z.W., Van Marck, E. and Merregaert, J. Expression and localization of CHODLdeltaE/CHODLfdeltaE, the soluble isoform of chondrolectin. Cell Biol. Int. 31 (2007) 1323–1330.

    PubMed  Article  CAS  Google Scholar 

  4. Weng, L., Van Bockstaele, D.R., Wauters, J., Van Marck, E., Plum, J., Berneman, Z.N. and Merregaert, J. A novel alternative spliced Chondrolectin isoform lacking the transmembrane domain is expressed during T cell maturation. J. Biol. Chem. 278 (2003) 19164–19170.

    PubMed  Article  CAS  Google Scholar 

  5. Drickamer, K. Ca2+-dependent carbohydrate-recognition domains in animal proteins. Curr. Opin. Struct. Biol. 3 (1993) 393–400.

    Article  CAS  Google Scholar 

  6. Drickamer, K. and Taylor, M.E. Biology of animal lectins. Annu. Rev. Cell. Biol. 9 (1993) 237–264.

    PubMed  Article  CAS  Google Scholar 

  7. Zelensky, A.N. and Gready, J.E. The C-type lectin-like domain superfamily. FEBS Lett. 272 (2005) 6179–6217.

    CAS  Google Scholar 

  8. Kresse, H. and Schönherr, E. Proteoglycans of the extracellular matrix and growth control. J. Cell. Physiol. J. Cell. Physiol. (2001) 266–274.

  9. Ellgaard, L. and Helenius, A. Quality control in the endoplasmic reticulum. Nat. Rev. 4 (2003) 181–191.

    Article  CAS  Google Scholar 

  10. Aronheim, A., Zandi, E., Hennemann, H., Elledge, S.J. and Karin, M. Isolation of an AP-1 repressor by a novel method for detecting proteinprotein interactions. Mol. Cell. Biol. 17 (1997) 3094–3102.

    PubMed  CAS  Google Scholar 

  11. Huang, W., Wang, S., Lozano, G. and de Crombrugghe, B. cDNA library screening using the Sos recruitment system. Biotechniques 30 (2001) 94–100.

    PubMed  CAS  Google Scholar 

  12. Beil, B., Screaton, G. and Stamm, S. Molecular cloning of htra2-beta-1 and htra2-beta-2, two human homologs of tra-2 generated by alternative splicing. DNA Cell Biol. 16 (1997) 679–690.

    PubMed  CAS  Google Scholar 

  13. Chinpaisal, C., Lee, C. and Wei, L. Studies of the mouse Rab geranylgeranyl transferase β-subunit: gene structure, expression and regulation. Gene 184 (1997) 237–243.

    PubMed  Article  CAS  Google Scholar 

  14. Armstrong, S.A., Seabra, M.C., Sudhof, T.C., Goldstein, J.L. and Brown, M.S. cDNA cloning and expression of the α and β subunits of Rat Rab geranylgeranyl transferase. J. Biol. Chem. 268 (1993) 12221–12229.

    PubMed  CAS  Google Scholar 

  15. Khosravi-Far, R., Clark, G.J., Abe, K., Cox, A.D., McLain, T., Lutz, R.J., Sinensky, M. and Der, C.J. Ras (CXXX) and Rab (CC/CXC) prenylation signal sequences are unique and functionally distinct. J. Biol. Chem. 267 (1992) 24363–24368.

    PubMed  CAS  Google Scholar 

  16. Leung, K.F., Baron, R., Ali, B.R., Magree, A.I. and Seabra, M.C. Rab GTPases containing a CAAX motif are processed post-geranylgeranylation by proteolysis and methylation. J. Biol. Chem. 282 (2007) 1487–1497.

    PubMed  Article  CAS  Google Scholar 

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Correspondence to Joseph Merregaert.

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Claessens, A., Weyn, C. & Merregaert, J. The cytoplasmic domain of chondrolectin interacts with the β-subunit of rab geranylgeranyl transferase. Cell Mol Biol Lett 13, 250–259 (2008).

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Key Words

  • C-type lectin
  • Chondrolectin
  • SRS