Abstract
Southern blot analysis of RT-PCR products from brain and heart revealed multiple products for a C-terminal region of Kir3.1. Sequencing yielded clones for wild-type Kir3.1 and three Kir3.1 C-terminal alternative splice variants, including a unique alternative exon. Two of these variants encoded truncated Kir3.1 molecules. Tissue distribution and electrophysiological characterization of a single truncated variant, Kir3.100 were then examined. Kir3.1 channels are gated by G-protein βγ-subunits binding to the C-terminal domain, thus, the truncation of Kir3.100 removes a major functional domain. When incorporated into heteromeric channels with other family members (Kir3.1, 3.2 or 3.4) several functional changes were observed: (1) Kir3.100 changes G-protein activation of Kir3 channels; (2) Kir3.100 is restricted in its ability to assemble with other channel subunits as heteromers; and (3) incorporation of Kir3.100 into heteromeric channel complexes alters the kinetics of channel re-activation.
Original language | English (US) |
---|---|
Pages (from-to) | 185-196 |
Number of pages | 12 |
Journal | Molecular Brain Research |
Volume | 46 |
Issue number | 1-2 |
DOIs | |
State | Published - Jun 1997 |
Keywords
- Dopamine
- Dopamine receptor
- G-protein
- Inward rectifier
- Kir3
- Oocyte
- Potassium channel
ASJC Scopus subject areas
- Molecular Biology
- Cellular and Molecular Neuroscience