Abstract：
:Molecular determinants of Ca2+ channel responsiveness to inhibition by receptor-coupled G proteins were investigated in Xenopus oocytes. The inhibitory response of alpha1B (N-type) channels was much larger than alpha1A (P/Q-type) channels, while alpha1C (L-type) channels were unresponsive. Differences in both degree and speed of inhibition were accounted for by variations in inhibitor off-rate. We tested proposals that inhibitory G protein and Ca2+ channel beta subunits compete specifically at the I-II loop. G protein-mediated inhibition remained unaltered in alpha1B subunits containing a point mutation in the I-II loop segment critical for Ca2+ channel beta subunit binding, and in chimeras where the I-II loop of alpha1B was replaced with counterparts from alpha1A or alpha1c. Full interconversion between modulatory behaviors of alpha1B and alpha1A was achieved only by swapping both motif I and the C-terminus in combination. Thus, essential structural elements for G protein modulation reside in multiple Ca2+ channel domains.
journal_name
Neuronjournal_title
Neuronauthors
Zhang JF,Ellinor PT,Aldrich RW,Tsien RWdoi
10.1016/s0896-6273(00)80229-9subject
Has Abstractpub_date
1996-11-01 00:00:00pages
991-1003issue
5eissn
0896-6273issn
1097-4199pii
S0896-6273(00)80229-9journal_volume
17pub_type
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