The cytoplasmic domain of chondrolectin interacts with the beta-subunit of Rab geranylgeranyl transferase
An Claessens1, Christine Weyn, Joseph Merregaert
1Laboratory of Molecular Biotechnology, Department of Biomedical Sciences, University of Antwerp, Universiteitsplein 1, B-2610, Wilrijk, Belgium.
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 ( f ), CHODL ( f Delta E ), CHODL ( Delta E )) 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.
Insights
Mouse chondrolectin (chodl), a transmembrane protein, interacts with Rab geranylgeranyl transferase beta-subunit (Rabggtb). This finding advances understanding of C-type lectin family functions in skeletal muscle, heart, and testes.
Area of Science:
- Molecular Biology
- Genetics
Background:
- Mouse chondrolectin (chodl) is the mouse homolog of human CHODL, a type Ia transmembrane protein.
- CHODL is expressed in human testis, prostate, heart, and skeletal muscle, with splice variants found in leukocytes.
- Chodl is predominantly expressed in adult mouse skeletal muscle, heart, testes, and lungs, and in embryonic tissues.
Purpose of the Study:
- To investigate the function of mouse chondrolectin (chodl) by identifying its protein interaction partners.
- To explore the biological roles of C-type lectin family members.
Main Methods:
- PCR-based subtractive cDNA library screening was used to isolate chodl.
- A complete Sos recruitment system (SRS) screen with the cytoplasmic domain of chodl was performed to identify interaction partners.
- In vitro transcription/translation and co-immunoprecipitation (co-IP) experiments were used to confirm protein interactions.
Main Results:
- The beta-subunit of Rab geranylgeranyl transferase (Rabggtb) was identified as a binding partner of chodl.
- Rabggtb was isolated multiple times during the SRS screen, indicating a strong interaction.
- The interaction between chodl and Rabggtb was validated through in vitro and co-IP experiments.
Conclusions:
- Mouse chondrolectin (chodl) interacts with Rab geranylgeranyl transferase beta-subunit (Rabggtb).
- This interaction provides insights into the functional roles of chondrolectin family proteins.
- Further research into chodl-Rabggtb interactions may elucidate their roles in skeletal muscle, heart, and testes biology.
Related Concept Videos
Rab Proteins
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
Rab Cascades
Assembly of Signaling Complexes
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Tail-anchoring of Proteins in the ER Membrane
Small GTPases - Ras and Rho
Three regulatory proteins control their activity:
Integrins
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
