GABAb trafficking

GABAb receptors are heterodimers. Two GABAb receptor subunits have been cloned, R1 and R2. Neither of these appears to express functional receptors on their own, but they are active when coexpressed, suggesting that a dimer is trafficked to the cell surface and forms an active complex. Evidence shows that the R1 subunit contains the GABA binding site while the R2 subunit interacts with the G protein [14]. 

Pagano, A., Rovelli, G., Mosbacher, J., et al. (2001) C-terminal interaction is essential for surface trafficking but not for heteromeric assembly of GABAb receptors. J. Neurosci. 21, 1189-1202. 

Margeta-Mitrovic M, Jan YN, Jan LY (2000) A trafficking checkpoint controls GABAb receptor heterodimerization. Neuron 27 97-106... 

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