Amino-terminus oligomerization regulates cardiac ryanodine receptor function

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N-terminus oligomerization regulates the function of cardiac ryanodine receptors.

The ryanodine receptor (RyR) is an ion channel composed of four identical subunits mediating calcium efflux from the endo/sarcoplasmic reticulum of excitable and non-excitable cells. We present several lines of evidence indicating that the RyR2 N-terminus is capable of self-association. A combination of yeast two-hybrid screens, co-immunoprecipitation analysis, chemical crosslinking and gel fil...

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Oligomerization of the cardiac ryanodine receptor C-terminal tail.

The C-terminal 100 amino acids of the RyR (ryanodine receptor), referred to as the C-terminal tail, is a highly conserved sequence that is present in all known RyR isoforms and which has been implicated in channel function. Deleting the final 15 amino acids from the full-length skeletal muscle RyR resulted in an inactive channel, attributed to impaired assembly of a tetrameric RyR complex [Gao,...

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Three-dimensional reconstruction of the recombinant type 3 ryanodine receptor and localization of its amino terminus.

Recombinant type 3 ryanodine receptor (RyR3) has been purified in quantities sufficient for structural characterization by cryoelectron microscopy and three-dimensional (3D) reconstruction. Two cDNAs were prepared and expressed in HEK293 cells, one encoding the wild-type RyR3 and the other encoding RyR3 containing glutathione S-transferase (GST) fused to its amino terminus (GST-RyR3). RyR3 was ...

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Adaptation of single cardiac ryanodine receptor channels.

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Catecholamine Interactions with the Cardiac Ryanodine Receptor

PDXScholar Dissertations and Theses Dissertations and Theses Let us know how access to this document benefits you. Abstract The cardiac ryanodine receptor (RyR2) is a Ca 2+ ion channel found in the sarcoplasmic reticulum (SR), an intracellular membranous Ca 2+ storage system. It is well known that a destabilization of RyR2 can lead to a Ca 2+ flux out of the SR, which results in an overload of ...

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ژورنال

عنوان ژورنال: Journal of Cell Science

سال: 2013

ISSN: 1477-9137,0021-9533

DOI: 10.1242/jcs.133538