PubMed 19665007
Referenced in: none
Automatically associated channels: Kv1.1 , Kv1.2 , Kv1.4 , Slo1
Title: Fast inactivation in potassium channels: an interplay of cytoplasmic domains.
Authors: Kavitha Sankaranarayanan, Hyder Usman, M K Mathew
Journal, date & volume: Biochem. Biophys. Res. Commun., 2009 Oct 23 , 388, 490-5
PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/19665007
Abstract
Fast inactivation in voltage-gated potassium channels has traditionally been associated exclusively with the N-terminus. Here, we explore the role of the T1 domain using a series of chimeric channels. A chimeric channel, 4N/2, (N-terminus from the rapidly inactivating hKv1.4, and the channel body from the non-inactivating hKv1.2), exhibited slower and incomplete inactivation as compared to the wild-type hKv1.4. Replacing the T1 domain of 4N2 with that from hKv1.2 (4N/2T1/2), restored inactivation, while that from hKv1.1 (4N/1T1/2) completely abolished inactivation. Based on these observations, we hypothesize a correlation between the tetramerization domain and the putative inactivation domain receptor in the process of rapid inactivation of hKv1 channels.