Baines, A.J. and Bennett, P.M. and Carter, Edward W. and Terracciano, Cesare M. (2009) Protein 4.1 and the control of ion channels. Blood Cell Molecules and Disease, 42 (3). pp. 211-215. ISSN 1079-9796 .
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The classical function of 4.1R in red blood cells is to contribute to the mechanochemical properties of the membrane by promoting the interaction between spectrin and actin. More recently, it has been recognized that 4.1R is required for the stable cell surface accumulation of a number of erythrocyte membrane proteins. 4.1R is one member of the mammalian 4.1 family - the others being 4.1N, 4.1G and 4.1B - and is expressed in many cell types other than erythrocytes. Recently we have examined the phenotype of hearts from 4.1R knockout mice. Although they had a generally normal morphology, these hearts exhibited bradycardia, and prolongation of both action potentials and QT intervals. Electrophysiological analysis revealed anomalies in a range of ion channel activities. In addition, the immunoreactivity of voltage-gated Na(+) channel NaV1.5 was reduced, indicating a role for 4.1R in the cellular accumulation of this ion channel. 4.1 proteins also have roles in the accumulation of at least two other classes of ion channel. In epithelia, 4.1 interacts with the store-operated channel TRPC4. In neurons, the ligand-gated channels GluR1 and GluR4 require 4.1 proteins for cell surface accumulation. The spectrum of transmembrane proteins that bind to 4.1 proteins overlaps with that of ankyrin. A hypothesis to investigate in the future is that differential regulation of 4.1 and ankyrins (e.g. by PIP(2)) allows highly selective control of cell surface accumulation and transport activity of a specific range of ion channels.
|Additional information:||Review Article|
|Uncontrolled keywords:||Erythrocyte; Cardiomyocyte; Heart rate; Cytoskeleton; Sodium channels|
|Subjects:||Q Science > QP Physiology (Living systems)|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||Anthony Baines|
|Date Deposited:||11 Sep 2009 10:14|
|Last Modified:||20 Apr 2012 11:07|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/18250 (The current URI for this page, for reference purposes)|
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