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* Residue conservation analysis
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DOI no:
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J Biol Chem
283:26676-26683
(2008)
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PubMed id:
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S100A1 and calmodulin compete for the same binding site on ryanodine receptor.
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N.T.Wright,
B.L.Prosser,
K.M.Varney,
D.B.Zimmer,
M.F.Schneider,
D.J.Weber.
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ABSTRACT
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In heart and skeletal muscle an S100 protein family member, S100A1, binds to the
ryanodine receptor (RyR) and promotes Ca(2+) release. Using competition binding
assays, we further characterized this system in skeletal muscle and showed that
Ca(2+)-S100A1 competes with Ca(2+)-calmodulin (CaM) for the same binding site on
RyR1. In addition, the NMR structure was determined for Ca(2+)-S100A1 bound to a
peptide derived from this CaM/S100A1 binding domain, a region conserved in RyR1
and RyR2 and termed RyRP12 (residues 3616-3627 in human RyR1). Examination of
the S100A1-RyRP12 complex revealed residues of the helical RyRP12 peptide
(Lys-3616, Trp-3620, Lys-3622, Leu-3623, Leu-3624, and Lys-3626) that are
involved in favorable hydrophobic and electrostatic interactions with
Ca(2+)-S100A1. These same residues were shown previously to be important for
RyR1 binding to Ca(2+)-CaM. A model for regulating muscle contraction is
presented in which Ca(2+)-S100A1 and Ca(2+)-CaM compete directly for the same
binding site on the ryanodine receptor.
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Selected figure(s)
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Figure 4.
FIGURE 4. Residues of the RyRP12 peptide (residues
3616-3627 or RyR1) and S100A1 involved in Ca^2^+-S100A1-RyRP12
complex formation. A, diagram illustrating hydrophobic residues
involved in the RyRP12-S100A1 interaction including Ala-53,
Ile-57, Leu-77, Ala-80, Leu-81, and Ala-84 of S100A1, and
Trp-3620, Leu-3623, and Leu-3624 of RyRP12. B, ribbon diagram
illustrating hydrophilic residues in the RyRP12-S100A1 complex
that are likely involved in ionic interactions, including Asp-52
and Glu-63 on S100A1 and Lys-3616, Lys-3622, and Lys-3627 on the
RyRP12 peptide. C, space-filling diagram of the S100A1-RyP12
peptide showing residues in green (Trp-3620 and Leu-3624) that
are important for calmodulin binding to the ryanodine receptor.
The rest of the RyRP12 peptide is colored in red, and the S100A1
subunits 1 and 2 are colored tan and blue, respectively. D,
ribbon diagram of the C-terminal region of CaM bound to the
CaMBD of the RyR (residues 3614-3643 of RyR; Protein Data Bank
code 2BCX) (17), showing side chains of the RyR that are
involved in ionic interactions with CaM; these same residues are
also likely to form salt bridges with negatively charged side
chains of Ca^2+-S100A1.
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Figure 5.
FIGURE 5. Schematic of S100A1 function in skeletal muscle.
Ca^2+-S100A1 and Ca^2+-CaM bind to an overlapping region of RyR1
(red) in a Ca^2+-dependent manner. S100A1 binding leads to
events that enhance SR calcium release. In contrast, calmodulin
binding to this CaM binding domain leads to events that reduce
SR calcium release. Competition between these two
calcium-binding proteins for this target site may regulate SR
Ca^2+ release in skeletal muscle. The asterisk close to the
Ca^2+-S100A1-RyRP12 structure denotes the location of the
residues of RyR that are C-terminal to RyRP12 (residues
3616-3627 of RyR) present in the longer RyR peptide (residues
3614-3643 of RyR), used for structural studies when bound to CaM.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2008,
283,
26676-26683)
copyright 2008.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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D.Rohde,
H.Brinks,
J.Ritterhoff,
G.Qui,
S.Ren,
and
P.Most
(2011).
S100A1 gene therapy for heart failure: A novel strategy on the verge of clinical trials.
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J Mol Cell Cardiol,
50,
777-784.
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D.W.Song,
J.G.Lee,
H.S.Youn,
S.H.Eom,
and
d.o. .H.Kim
(2011).
Ryanodine receptor assembly: A novel systems biology approach to 3D mapping.
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Prog Biophys Mol Biol,
105,
145-161.
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B.Gilquin,
B.R.Cannon,
A.Hubstenberger,
B.Moulouel,
E.Falk,
N.Merle,
N.Assard,
S.Kieffer,
D.Rousseau,
P.T.Wilder,
D.J.Weber,
and
J.Baudier
(2010).
The calcium-dependent interaction between S100B and the mitochondrial AAA ATPase ATAD3A and the role of this complex in the cytoplasmic processing of ATAD3A.
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Mol Cell Biol,
30,
2724-2736.
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D.B.Zimmer,
and
D.J.Weber
(2010).
The Calcium-Dependent Interaction of S100B with Its Protein Targets.
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Cardiovasc Psychiatry Neurol,
2010,
0.
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I.Matsuura,
C.Y.Lai,
and
K.N.Chiang
(2010).
Functional interaction between Smad3 and S100A4 (metastatin-1) for TGF-beta-mediated cancer cell invasiveness.
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Biochem J,
426,
327-335.
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I.N.Pessah,
G.Cherednichenko,
and
P.J.Lein
(2010).
Minding the calcium store: Ryanodine receptor activation as a convergent mechanism of PCB toxicity.
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Pharmacol Ther,
125,
260-285.
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M.Völkers,
D.Rohde,
C.Goodman,
and
P.Most
(2010).
S100A1: a regulator of striated muscle sarcoplasmic reticulum Ca2+ handling, sarcomeric, and mitochondrial function.
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J Biomed Biotechnol,
2010,
178614.
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B.A.McGivney,
S.S.Eivers,
D.E.MacHugh,
J.N.MacLeod,
G.M.O'Gorman,
S.D.Park,
L.M.Katz,
and
E.W.Hill
(2009).
Transcriptional adaptations following exercise in thoroughbred horse skeletal muscle highlights molecular mechanisms that lead to muscle hypertrophy.
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BMC Genomics,
10,
638.
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C.Kraus,
D.Rohde,
C.Weidenhammer,
G.Qiu,
S.T.Pleger,
M.Voelkers,
M.Boerries,
A.Remppis,
H.A.Katus,
and
P.Most
(2009).
S100A1 in cardiovascular health and disease: closing the gap between basic science and clinical therapy.
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J Mol Cell Cardiol,
47,
445-455.
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E.O.Hernández-Ochoa,
B.L.Prosser,
N.T.Wright,
M.Contreras,
D.J.Weber,
and
M.F.Schneider
(2009).
Augmentation of Cav1 channel current and action potential duration after uptake of S100A1 in sympathetic ganglion neurons.
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Am J Physiol Cell Physiol,
297,
C955-C970.
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N.T.Wright,
B.R.Cannon,
P.T.Wilder,
M.T.Morgan,
K.M.Varney,
D.B.Zimmer,
and
D.J.Weber
(2009).
Solution structure of S100A1 bound to the CapZ peptide (TRTK12).
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J Mol Biol,
386,
1265-1277.
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P.A.Lobo,
and
F.Van Petegem
(2009).
Crystal structures of the N-terminal domains of cardiac and skeletal muscle ryanodine receptors: insights into disease mutations.
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Structure,
17,
1505-1514.
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PDB codes:
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N.T.Wright,
K.G.Inman,
J.A.Levine,
B.R.Cannon,
K.M.Varney,
and
D.J.Weber
(2008).
Refinement of the solution structure and dynamic properties of Ca(2+)-bound rat S100B.
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J Biomol NMR,
42,
279-286.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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