Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

Heteromultimerization between different inwardly rectifying (Kir) potassium channel subunits is an important mechanism for the generation of functional diversity. However, little is known about the mechanisms that control this process and that prevent promiscuous interactions in cells that express many different Kir subunits. In this study, we have examined the heteromeric assembly of Kir5.1 with other Kir subunits and have shown that this subunit exhibits a highly selective interaction with members of the Kir4.0 subfamily and does not physically associate with other Kir subunits such as Kir1.1, Kir2.1, and Kir6.2. Furthermore, we have identified regions within the Kir4.1 subunit that appear to govern the specificity of this interaction. These results help us to understand the mechanisms that control Kir subunit recognition and assembly and how cells can express many different Kir channels while maintaining distinct subpopulations of homo- and heteromeric channels within the cell.

Original publication

DOI

10.1152/ajpcell.00479.2002

Type

Journal article

Journal

Am J Physiol Cell Physiol

Publication Date

04/2003

Volume

284

Pages

C910 - C917

Keywords

Amino Acid Sequence, Animals, Female, Mice, Molecular Sequence Data, Oocytes, Potassium Channels, Potassium Channels, Inwardly Rectifying, Protein Processing, Post-Translational, Protein Structure, Tertiary, Rats, Xenopus laevis