Transmembrane domain self-association of neuronal membrane glycoprotein, M6a

FORMOSO, K; CAMILA SCORTICATI; FRASCH, AC.

Puerto Madryn

Congreso; 46th Annual Meeting-Argentine Society for Biochemistry and Molecular Biology Research; 2010

Biocell

GPM6A is a stress/antidepressant-responsive gene in the hippocampus of different animal models. This gene is down regulated in both physically and socially stressed animals. M6a regulates neurite/filopodium outgrowth in hippocampal neuronal culture through an unknown mechanism. It is well known that self-association of membrane proteins is important in the regulation of extra and intracellular signaling pathways. M6a is a protein with four transmembrane domains. Demonstrating the existence of protein-protein interactions of M6a in rat hippocampus could give us a clue of how this protein exerts its function. To this end, a chemical crosslinking assay and an in vitro homodimerization of TMs using TOXCAT system were performed. We tested for the formation of stable M6a oligomers in the presence/absence of chemical cross-linkers and we found that M6a forms different stable multimers. The TOXCAT oligomerization assay showed that there is self-interaction among all M6a TMS. These results allow us to conclude that M6a forms oligomers probably interacting through its TMS and that this interaction might be an important step on M6a activation.