Ubiquitous SPRY domains and their role in the skeletal type ryanodine receptor
Date
2009
Authors
Tae, Han Shen
Casarotto, Marco
Dulhunty, Angela
Journal Title
Journal ISSN
Volume Title
Publisher
Springer
Abstract
We recently identified the second of three SPRY domains in the skeletal muscle ryanodine receptor type 1 (RyR1) as a potential binding partner in the RyR1 ion channel for the recombinant II-III loop of the skeletal muscle dihydropyridine receptor, for a scorpion toxin, Imperatoxin A and for an interdomain interaction within RyR1. SPRY domains are structural domains that were first described in the fungal Dictyostelium discoideum tyrosine kinase spore lysis A and all three isoforms of the mammalian ryanodine receptor (RyR). Our studies are the first to assign a function to any of the three SPRY domains in the RyR. However, in other systems SPRY domains provide binding sites for regulatory proteins or intramolecular binding sites that maintain the structural integrity of a protein. In this article, we review the general characteristics of a range of SPRY domains and discuss evidence that the SPRY2 domain in RyR1 supports interactions with binding partners that contain a structural surface of aligned basic residues.
Description
Keywords
Keywords: 1,4 dihydropyridine receptor; imperatoxin A; marine toxin; protein tyrosine kinase; ryanodine receptor; ryanodine receptor 1; scorpion venom; sprouty protein; unclassified drug; binding site; calcium signaling; Dictyostelium discoideum; excitation contrac Calcium signalling; Excitation-contraction coupling; Protein-protein interactions; Ryanodine receptor; Skeletal muscle; SPRY domains
Citation
Collections
Source
European Biophysics Journal
Type
Journal article
Book Title
Entity type
Access Statement
License Rights
Restricted until
2037-12-31
Downloads
File
Description