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First published online May 24, 2006
doi: 10.1242/10.1242/jcs.02936

Journal of Cell Science 119, 2386-2397 (2006)
Published by The Company of Biologists 2006
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Research Article

Ryanodine receptor interaction with the SNARE-associated protein snapin

Spyros Zissimopoulos1,*, Duncan J. West2, Alan J. Williams2 and F. Anthony Lai1

1 Wales Heart Research Institute, Department of Cardiology, Cardiff University School of Medicine, Heath Park, Cardiff, CF14 4XN, UK
2 Department of Cardiac Medicine, NHLI, Imperial College London, Dovehouse Street, London, SW3 6LY, UK

* Author for correspondence (e-mail: ZissimopoulosS{at}cardiff.ac.uk)

Accepted 14 February 2006

The ryanodine receptor (RyR) is a widely expressed intracellular calcium (Ca2+)-release channel regulating processes such as muscle contraction and neurotransmission. Snapin, a ubiquitously expressed SNARE-associated protein, has been implicated in neurotransmission. Here, we report the identification of snapin as a novel RyR2-interacting protein. Snapin binds to a 170-residue predicted ryanodine receptor cytosolic loop (RyR2 residues 4596-4765), containing a hydrophobic segment required for snapin interaction. Ryanodine receptor binding of snapin is not isoform specific and is conserved in homologous RyR1 and RyR3 fragments. Consistent with peptide fragment studies, snapin interacts with the native ryanodine receptor from skeletal muscle, heart and brain. The snapin-RyR1 association appears to sensitise the channel to Ca2+ activation in [3H]ryanodine-binding studies. Deletion analysis indicates that the ryanodine receptor interacts with the snapin C-terminus, the same region as the SNAP25-binding site. Competition experiments with native ryanodine receptor and SNAP25 suggest that these two proteins share an overlapping binding site on snapin. Thus, regulation of the association between ryanodine receptor and snapin might constitute part of the elusive molecular mechanism by which ryanodine-sensitive Ca2+ stores modulate neurosecretion.

Key words: Ryanodine receptor, Snapin, SNARE complex, Protein interaction, Neurosecretion


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