[Protein-protein interactions in membranes: concepts and the example of calcium ATPase from the sarcoplasmic reticulum]

Abstract

The organization of polypeptide chains in the membrane has attracted widespread interest. This is particularly true for transport proteins: indeed, the existence of a quaternary structure may obviously have important implications for the mechanism of solute transport through the membrane. The problem arises from the fact that it is extremely difficult to demonstrate unambiguously that a protein is truly oligomeric in the membrane. In this paper various techniques are considered, either direct methods of investigation such as X-ray or neutron scattering, ESR, and radiation inactivation, or indirect methods (primarily the solubilization of the protein by non-denaturing detergents). In very few cases the existence of a 'structural' oligomer has been demonstrated. However, the question remains whether the oligomer also has a functional role, i.e., is it directly necessary for example to form a hydrophilic pathway for an ion, or indirectly to stabilize the enzyme structure or to allow a control to take place at a certain defined step of the transport cycle?.