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.

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 Proteins01:14

Rab Proteins

Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
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 Cascades01:25

Rab Cascades

Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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 Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity:
Integrins01:10

Integrins

Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
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,...