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Homer and the ryanodine receptor

Date

2009

Authors

Pouliquin, Pierre
Dulhunty, Angela

Journal Title

Journal ISSN

Volume Title

Publisher

Springer

Abstract

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.

Description

Keywords

Keywords: calcium ion; ion channel; protein homer; ryanodine receptor; ryanodine receptor 1; ryanodine receptor 2; ryanodine receptor 3; binding affinity; calcium transport; heart muscle; ligand binding; mammal; nerve cell; nonhuman; protein protein interaction; re Homer; Protein targeting; Protein-protein interactions; Ryanodine receptors

Citation

Source

European Biophysics Journal

Type

Journal article

Book Title

Entity type

Access Statement

License Rights

DOI

10.1007/s00249-009-0494-1

Restricted until

2037-12-31