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Oligomerization at the Membrane

Potassium Channel Structure and Function

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Book cover Protein Dimerization and Oligomerization in Biology

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 747))

Abstract

Cell membranes present a naturally impervious barrier to aqueous solutes, such that the physiochemical environment on either side of the lipid bilayer can substantially differ. Integral membrane proteins are embedded in this heterogeneous lipid environment, wherein the juxtaposition of apolar and polar molecular surfaces defines factors such as transverse orientation, the surface area available for oligomerisation and the symmetry of resultant assemblies. This chapter focuses on potassium channels —representative molecular pores that play a critical role in electrical signalling by enabling selective transport of K+ ions across cell membranes. Oligomerization is central to K+ channel action; individual subunits are nonfunctional and conduction, selectivity and gating involve manipulation of the common subunit interface of the tetramer. Regulation of channel activity can be viewed from the perspective that the pore of K+ channels has coopted other proteins, utilizing a process of hetero-oligomerisation to absorb new functions that both enable the pore to respond to extrinsic signals and provide an electrical signature.

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Authors and Affiliations

  1. The Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria, Australia

    Oliver B. Clarke & Jacqueline M. Gulbis

  2. Department of Medical Biology, The University of Melbourne, Melbourne, Victoria, Australia

    Oliver B. Clarke & Jacqueline M. Gulbis

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  1. Oliver B. Clarke
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Correspondence to Jacqueline M. Gulbis .

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  1. School of Molecular Bioscience, University of Sydney, Sydney, Australia

    Jacqueline M. Matthews PhD

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Clarke, O.B., Gulbis, J.M. (2012). Oligomerization at the Membrane. In: Matthews, J.M. (eds) Protein Dimerization and Oligomerization in Biology. Advances in Experimental Medicine and Biology, vol 747. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-3229-6_8

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