Abstract:
:In response to changes in membrane potential, voltage-dependent ion channel proteins undergo conformational rearrangements that lead to channel opening. These rearrangements move a net charge, measured as "gating current", across the membrane. Here we characterize the effects of the pharmacological blocker 4-aminopyridine on both the K+ and gating currents of wild-type and mutant Shaker K+ channels. Our results indicate that the activation of these channels involves two distinct types of structural rearrangement. In addition to independent Hodgkin and Huxley type rearrangements for each of the four subunits, which are responsible for most of the gating charge movement, Shaker channels interconvert between two quaternary conformations during activation. The transition between the two quaternary states moves about 10% of the total gating charge, and it is selectively blocked by 4-aminopyridine.
journal_name
Neuronjournal_title
Neuronauthors
McCormack K,Joiner WJ,Heinemann SHdoi
10.1016/0896-6273(94)90273-9subject
Has Abstractpub_date
1994-02-01 00:00:00pages
301-15issue
2eissn
0896-6273issn
1097-4199pii
0896-6273(94)90273-9journal_volume
12pub_type
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