Abstract
Excitation-contraction coupling in heart muscle requires the activation of Ca2+-release channels/type 2 ryanodine receptors (RyR2s) by Ca2+ influx. RyR2s are arranged on the sarcoplasmic reticular membrane in closely packed arrays such that their large cytoplasmic domains contact one another. We now show that multiple RyR2s can be isolated under conditions such that they remain physically coupled to one another. When these coupled channels are examined in planar lipid bilayers, multiple channels exhibit simultaneous gating, termed "coupled gating." Removal of the regulatory subunit, the FK506 binding protein (FKBP12.6), functionally but not physically uncouples multiple RyR2 channels. Coupled gating between RyR2 channels may be an important regulatory mechanism in excitation-contraction coupling as well as in other signaling pathways involving intracellular Ca2+ release.
Original language | English (US) |
---|---|
Pages (from-to) | 1151-1158 |
Number of pages | 8 |
Journal | Circulation Research |
Volume | 88 |
Issue number | 11 |
State | Published - Jun 8 2001 |
Externally published | Yes |
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Keywords
- Ca channels
- Coupled gating
- Excitation-contraction coupling
- FKBP12.6
- Ryanodine receptors
ASJC Scopus subject areas
- Physiology
- Cardiology and Cardiovascular Medicine
Cite this
Coupled gating between cardiac calcium release channels (ryanodine receptors). / Marx, Steven O.; Gaburjakova, Jana; Gaburjakova, Marta; Henrikson, Charles; Ondrias, Karol; Marks, Andrew R.
In: Circulation Research, Vol. 88, No. 11, 08.06.2001, p. 1151-1158.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Coupled gating between cardiac calcium release channels (ryanodine receptors)
AU - Marx, Steven O.
AU - Gaburjakova, Jana
AU - Gaburjakova, Marta
AU - Henrikson, Charles
AU - Ondrias, Karol
AU - Marks, Andrew R.
PY - 2001/6/8
Y1 - 2001/6/8
N2 - Excitation-contraction coupling in heart muscle requires the activation of Ca2+-release channels/type 2 ryanodine receptors (RyR2s) by Ca2+ influx. RyR2s are arranged on the sarcoplasmic reticular membrane in closely packed arrays such that their large cytoplasmic domains contact one another. We now show that multiple RyR2s can be isolated under conditions such that they remain physically coupled to one another. When these coupled channels are examined in planar lipid bilayers, multiple channels exhibit simultaneous gating, termed "coupled gating." Removal of the regulatory subunit, the FK506 binding protein (FKBP12.6), functionally but not physically uncouples multiple RyR2 channels. Coupled gating between RyR2 channels may be an important regulatory mechanism in excitation-contraction coupling as well as in other signaling pathways involving intracellular Ca2+ release.
AB - Excitation-contraction coupling in heart muscle requires the activation of Ca2+-release channels/type 2 ryanodine receptors (RyR2s) by Ca2+ influx. RyR2s are arranged on the sarcoplasmic reticular membrane in closely packed arrays such that their large cytoplasmic domains contact one another. We now show that multiple RyR2s can be isolated under conditions such that they remain physically coupled to one another. When these coupled channels are examined in planar lipid bilayers, multiple channels exhibit simultaneous gating, termed "coupled gating." Removal of the regulatory subunit, the FK506 binding protein (FKBP12.6), functionally but not physically uncouples multiple RyR2 channels. Coupled gating between RyR2 channels may be an important regulatory mechanism in excitation-contraction coupling as well as in other signaling pathways involving intracellular Ca2+ release.
KW - Ca channels
KW - Coupled gating
KW - Excitation-contraction coupling
KW - FKBP12.6
KW - Ryanodine receptors
UR - http://www.scopus.com/inward/record.url?scp=0035827726&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035827726&partnerID=8YFLogxK
M3 - Article
C2 - 11397781
AN - SCOPUS:0035827726
VL - 88
SP - 1151
EP - 1158
JO - Circulation Research
JF - Circulation Research
SN - 0009-7330
IS - 11
ER -