Homer and the ryanodine receptor.
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.
Pouliquin
Pierre
P
Division of Molecular Bioscience, John Curtin School of Medical Research, Australian National University, PO Box 334, Canberra, ACT, 2601, Australia.
Dulhunty
Angela Fay
AF
D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism; D000072233:Homer Scaffolding Proteins; D006801:Humans; D042541:Intracellular Space / Q000378:metabolism; D008024:Ligands; D008969:Molecular Sequence Data; D021381:Protein Transport; D019837:Ryanodine Receptor Calcium Release Channel / Q000737:chemistry / Q000378:metabolism
D002352:Carrier Proteins; D000072233:Homer Scaffolding Proteins; D008024:Ligands; D019837:Ryanodine Receptor Calcium Release Channel