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Homer and the ryanodine receptor

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Homer proteins have recently been identified as novel high-affinity ligands that modulate ryanodine receptor (RyR) Ca2+ release channels in heart and skeletal muscle, through an EVH1 domain which binds to proline-rich regions in target proteins. Many Homer proteins can also self-associate through a coiled-coil domain that allows their multimerisation. In other tissues, especially neurons, Homer anchors proteins embedded in the surface membrane to the Ca2+ release channel in the endoplasmic reticulum and can anchor membrane or cytosolic proteins to the cytoskeleton. Although this anchoring aspect of Homer function has not been extensively investigated in muscle, there are consensus sequences for Homer binding in the RyR and on many of the proteins that it interacts with in the massive RyR ion channel complex. In this review we explore the potential of Homer to contribute to a variety of cell processes in muscle and neurons that also involve RyR channels.

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Correspondence to Angela Fay Dulhunty.

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“Proteins, membranes and cells: the structure-function nexus”. Contributions from the annual scientific meeting (including a special symposium in honour of Professor Alex Hope of Flinders University, South Australia) of the Australian Society for Biophysics held in Canberra, ACT, Australia, 28 September–1 October 2008.

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Pouliquin, P., Dulhunty, A.F. Homer and the ryanodine receptor. Eur Biophys J 39, 91–102 (2009).

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