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M306645200v1
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Papers In Press, published online ahead of print September 24, 2003
J. Biol. Chem, 10.1074/jbc.M306645200
Submitted on June 23, 2003
Revised on September 22, 2003
Accepted on September 24, 2003

Competitive and synergistic interactions of G protein beta 2 and Ca2+ channel beta 1b subunits with CaV2.1 channels, revealed by mammalian two-hybrid and FRET measurementss

Alexander Hümmer, Oliver Delzeith, Shannon R. Gomez, Rosa L. Moreno, Melanie D. Mark, and Stefan Herlitze

Neurosciences Dept., Case Western Reserve University, Cleveland, OH 44106

Corresponding Author: sxh106{at}pop.cwru.edu

Presynaptic Ca2+ channels are inhibited by metabotropic receptors. A possible mechanism for this inhibition is that G protein beta gamma subunits modulate the binding of the Ca2+ channel beta subunit on the Ca2+ channel complex a nd induce a conformational state from which channel opening is more reluctant. To test this hypothesis we analyzed the binding of Ca2+ channel beta and G protein beta subunit on the two separate binding sites, i.e. the loopI-II and the C-termin us, and on the full length P/Q-type alpha 12.1 subunit by using a modified mammalian two hybrid system and FRET measurements. Analysis of the interactions on the isolated bindings sites revealed that the Ca2+ channel beta 1b subunit ind uces a strong fluorescent signal when interacting with the loopI-II, but not with the C-terminus. In contrast, the G protein beta subunit induces FRET signals on both the C-terminus and loopI-II. Analysis of the interactions on the full length channel i ndicates that Ca2+ channel beta 1b and G protein beta subunits bind to the alpha 1 subunit at the same time. Coexpression of the G protein increases the FRET signal between alpha 1/beta 1b FRET pairs but not for alpha 1/beta 1b FRET pairs where the C-terminus was deleted from the alpha 1 subunit. The results suggest that the G protein alters the orientation and/or association between the Ca2+ channel beta and alpha 12.1 subunits, which involves the C-terminus of the alpha 1 subunit and may corresponds to a new conformational state of the channel.Ï


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