Abstract
Ryanodine receptor 1 (RyR1, the sarcoplasmic reticulum Ca2+ release channel) and α1sdihydropyridine receptor (DHPR, the surface membrane voltage sensor) of skeletal muscle belong to separate membrane systems but are functionally and structurally linked. Four α 1sDHPRs associated with the four identical subunits of a RyR form a tetrad. We treated skeletal muscle cell lines with ryanodine, at concentrations that block RyRs, and determined whether this treatment affects the distance between DHPRs in the tetrad. We find a substantial (≈2-nm) shift in the α1sDHPR positions, indicating that ryanodine induces large conformational changes in the RyR1 cytoplasmic domain and that the α1sDHPR-RyR complex acts as a unit.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 12748-12752 |
| Number of pages | 5 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 101 |
| Issue number | 34 |
| DOIs | |
| State | Published - Aug 24 2004 |
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Keywords
- Dihydropyridine receptors
- E4032A mutant ryanodine receptor
- Ryanodine
- Ryanodine receptors
- Skeletal muscle
ASJC Scopus subject areas
- Genetics
- General
Cite this
Evidence for conformational coupling between two calcium channels. / Paolini, C.; Fessenden, James D.; Pessah, Isaac N; Franzini-Armstrong, C.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 101, No. 34, 24.08.2004, p. 12748-12752.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Evidence for conformational coupling between two calcium channels
AU - Paolini, C.
AU - Fessenden, James D.
AU - Pessah, Isaac N
AU - Franzini-Armstrong, C.
PY - 2004/8/24
Y1 - 2004/8/24
N2 - Ryanodine receptor 1 (RyR1, the sarcoplasmic reticulum Ca2+ release channel) and α1sdihydropyridine receptor (DHPR, the surface membrane voltage sensor) of skeletal muscle belong to separate membrane systems but are functionally and structurally linked. Four α 1sDHPRs associated with the four identical subunits of a RyR form a tetrad. We treated skeletal muscle cell lines with ryanodine, at concentrations that block RyRs, and determined whether this treatment affects the distance between DHPRs in the tetrad. We find a substantial (≈2-nm) shift in the α1sDHPR positions, indicating that ryanodine induces large conformational changes in the RyR1 cytoplasmic domain and that the α1sDHPR-RyR complex acts as a unit.
AB - Ryanodine receptor 1 (RyR1, the sarcoplasmic reticulum Ca2+ release channel) and α1sdihydropyridine receptor (DHPR, the surface membrane voltage sensor) of skeletal muscle belong to separate membrane systems but are functionally and structurally linked. Four α 1sDHPRs associated with the four identical subunits of a RyR form a tetrad. We treated skeletal muscle cell lines with ryanodine, at concentrations that block RyRs, and determined whether this treatment affects the distance between DHPRs in the tetrad. We find a substantial (≈2-nm) shift in the α1sDHPR positions, indicating that ryanodine induces large conformational changes in the RyR1 cytoplasmic domain and that the α1sDHPR-RyR complex acts as a unit.
KW - Dihydropyridine receptors
KW - E4032A mutant ryanodine receptor
KW - Ryanodine
KW - Ryanodine receptors
KW - Skeletal muscle
UR - http://www.scopus.com/inward/record.url?scp=4344607999&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=4344607999&partnerID=8YFLogxK
U2 - 10.1073/pnas.0404836101
DO - 10.1073/pnas.0404836101
M3 - Article
C2 - 15310845
AN - SCOPUS:4344607999
VL - 101
SP - 12748
EP - 12752
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 34
ER -