Homer and the ryanodine receptor

被引:34
|
作者
Pouliquin, Pierre [1 ]
Dulhunty, Angela Fay [1 ]
机构
[1] Australian Natl Univ, John Curtin Sch Med Res, Div Mol Biosci, Canberra, ACT 2601, Australia
来源
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS | 2009年 / 39卷 / 01期
关键词
Homer; Ryanodine receptors; Protein-protein interactions; Protein targeting; METABOTROPIC GLUTAMATE RECEPTORS; CA2+ RELEASE CHANNEL; SKELETAL-MUSCLE; CALCIUM-RELEASE; DIHYDROPYRIDINE RECEPTORS; SARCOPLASMIC-RETICULUM; PROTEIN-KINASE; FUNCTIONAL INTERACTION; ENDOPLASMIC-RETICULUM; POSTSYNAPTIC DENSITY;
D O I
10.1007/s00249-009-0494-1
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
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.
引用
收藏
页码:91 / 102
页数:12
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