Abstract
Through the collaborative actions of b-spectrin and ankyrin, a cytoskeletal adaptor protein, integral and peripheral membrane proteins find order and stability in the relatively fluid environment of the plasma membrane. Not only is the ankyrin/β-spectrin complex responsible for the proper targeting and retention of membrane proteins but it facilitates the formation of multi-protein complexes to maximize local signaling between membrane and effector proteins. Dysfunction in ankyrin or β-spectrin causes deficiencies in fundamental cellular properties such as membrane stability, excitability, and adhesion. This review focuses on the direct effects of ankyrin function on membrane proteins in terms of binding and stability, intracellular transport, membrane targeting and retention, and altered biophysical properties. We propose that ankyrin and β-spectrin are important for the normal progression of many membrane proteins along their biosynthetic pathway from stabilizing the membrane protein to it’s proper trafficking and eventual targeting and retention at membrane domains. The second half of the review addresses how an ankyrin/membrane protein interaction influences the local membrane environment with particular emphasis on membrane stability, membrane domain formation, and membrane domain specialization. We propose that not only are ankyrins necessary for erythroid membrane stability but they are required in some cells types for membrane domain formation and integral for the formation of specialized membrane domains in myocytes.
Highlights
Membrane proteins facilitate a variety of interactions between the external and internal cellular environments including the transport or exchange of ions and molecules, cellular adherence to a surrounding substrate or neighboring cell, and the translation of an extracellular signal into an altered cellular response
Since the initial discovery of the ankyrin/β-spectrin cytoskeletal complex some 35 years ago, there has been a tremendous growth in our understanding of how this complex functions in both normal and diseased states
Ankyrin dysfunction was only associated with haemolytic anemia, but dysfunction of ankyrin and associated proteins has been connected to numerous cardiac arrhythmias, epilepsy, bipolar disorder, and a type of neonatal diabetes
Summary
Membrane proteins facilitate a variety of interactions between the external and internal cellular environments including the transport or exchange of ions and molecules, cellular adherence to a surrounding substrate or neighboring cell, and the translation of an extracellular signal into an altered cellular response. Ankyrins are adaptor proteins that link membrane proteins to the underlying cytoskeleton. This review is organized around two central themes: ankyrin function on membrane proteins and the cellular effects of ankyrin/ membrane protein interactions. Ankyrins serve as an interface between membrane-bound proteins and the underlying cytoskeleton This interaction contributes to the stability of the membrane protein’s location and expression within the plasma membrane. Isoforms of ankyrin-B and ankyrin-G have been detected in a greater variety of tissues While some tissues such as the heart and cerebellum display all three ankyrin gene products, they are not functionally redundant, i.e. ankyrin-G cannot compensate for the loss of ankyrin-B in cardiomyocytes [1].
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