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Updated: Jun 22, 2026

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
Published on: November 30, 2018
Homer and the ryanodine receptor
Pierre Pouliquin1, Angela Fay Dulhunty
1Division of Molecular Bioscience, John Curtin School of Medical Research, Australian National University, PO Box 334, Canberra, ACT, 2601, Australia.
Abstract:
Homer proteins have recently been identified as novel high-affinity ligands that modulate ryanodine receptor (RyR) Ca(2+) 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 Ca(2+) 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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