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STAC3 incorporation into skeletal muscle triads occurs independent of the dihydropyridine receptor

Published on Dec 1, 2018in Journal of Cellular Physiology4.522
· DOI :10.1002/jcp.26767
Marta Campiglio10
Estimated H-index: 10
,
Mehmet Mahsum Kaplan2
Estimated H-index: 2
,
Bernhard E. Flucher37
Estimated H-index: 37
Abstract
: Excitation-contraction (EC) coupling in skeletal muscles operates through a physical interaction between the dihydropyridine receptor (DHPR), acting as a voltage sensor, and the ryanodine receptor (RyR1), acting as a calcium release channel. Recently, the adaptor protein SH3 and cysteine-rich containing protein 3 (STAC3) has been identified as a myopathy disease gene and as an additional essential EC coupling component. STAC3 interacts with DHPR sequences including the critical EC coupling domain and has been proposed to function in linking the DHPR and RyR1. However, we and others demonstrated that incorporation of recombinant STAC3 into skeletal muscle triads critically depends only on the DHPR but not the RyR1. On the contrary, here, we provide evidence that endogenous STAC3 incorporates into triads in the absence of the DHPR in myotubes and muscle fibers of dysgenic mice. This finding demonstrates that STAC3 interacts with additional triad proteins and is consistent with its proposed role in directly or indirectly linking the DHPR with the RyR1.
  • References (26)
  • Citations (2)
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References26
Newest
#1Alexander Polster (University of Colorado Denver)H-Index: 6
#2Benjamin R. Nelson (UTSW: University of Texas Southwestern Medical Center)H-Index: 8
Last. Kurt G. Beam (University of Colorado Denver)H-Index: 50
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In skeletal muscle, residues 720–764/5 within the Ca V 1.1 II–III loop form a critical domain that plays an essential role in transmitting the excitation–contraction (EC) coupling Ca 2+ release signal to the type 1 ryanodine receptor (RyR1) in the sarcoplasmic reticulum. However, the identities of proteins that interact with the loop and its critical domain and the mechanism by which the II–III loop regulates RyR1 gating remain unknown. Recent work has shown that EC coupling in skeletal muscle o...
12 CitationsSource
The adaptor proteins STAC1, STAC2, and STAC3 represent a newly identified family of regulators of voltage-gated calcium channel (CaV) trafficking and function. The skeletal muscle isoform STAC3 is essential for excitation–contraction coupling and its mutation causes severe muscle disease. Recently, two distinct molecular domains in STAC3 were identified, necessary for its functional interaction with CaV1.1: the C1 domain, which recruits STAC proteins to the calcium channel complex in skeletal mu...
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#1Stefano Perni (Anschutz Medical Campus)H-Index: 13
#2Manuela Lavorato (UPenn: University of Pennsylvania)H-Index: 5
Last. Kurt G. Beam (Anschutz Medical Campus)H-Index: 50
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Abstract Skeletal muscle contraction is triggered by Ca2+ release from the sarcoplasmic reticulum (SR) in response to plasma membrane (PM) excitation. In vertebrates, this depends on activation of the RyR1 Ca2+ pore in the SR, under control of conformational changes of CaV1.1, located ∼12 nm away in the PM. Over the last ∼30 y, gene knockouts have revealed that CaV1.1/RyR1 coupling requires additional proteins, but leave open the possibility that currently untested proteins are also necessary. H...
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#1Siobhan M. Wong King Yuen (UBC: University of British Columbia)H-Index: 3
#2Marta Campiglio (Innsbruck Medical University)H-Index: 10
Last. Filip Van Petegem (UBC: University of British Columbia)H-Index: 29
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Excitation–contraction (EC) coupling in skeletal muscle requires functional and mechanical coupling between L-type voltage-gated calcium channels (Ca V 1.1) and the ryanodine receptor (RyR1). Recently, STAC3 was identified as an essential protein for EC coupling and is part of a group of three proteins that can bind and modulate L-type voltage-gated calcium channels. Here, we report crystal structures of tandem-SH3 domains of different STAC isoforms up to 1.2-A resolution. These form a rigid int...
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Last. Joerg Striessnig (University of Innsbruck)H-Index: 21
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Ca 2+ -influx through L-type Ca 2+ -channels (LTCCs) is associated with activity-related stressful oscillations of Ca 2+ -levels within dopaminergic (DA) neurons in the substantia nigra (SN), which may contribute to their selective degeneration in Parkinson9s disease (PD). LTCC blockers were neuroprotective in mouse neurotoxin models of PD and isradipine is currently undergoing testing in a phase-III clinical trial in early PD. We report no evidence for neuroprotection by in vivo pretreatment wi...
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#1Marta Campiglio (Innsbruck Medical University)H-Index: 10
#2Bernhard E. Flucher (Innsbruck Medical University)H-Index: 37
The adaptor protein STAC3 is essential for skeletal muscle excitation-contraction (EC) coupling and a mutation in the STAC3 gene has been linked to a severe muscle disease, Native American myopathy (NAM). However the function of STAC3, its interaction partner, and the mode of interaction within the EC-coupling complex remained elusive. Here we demonstrate that STAC3 forms a stable interaction with the voltage-sensor of EC-coupling, CaV1.1, and that this interaction depends on a hitherto unidenti...
18 CitationsSource
#1Jeremy W. Linsley (UM: University of Michigan)H-Index: 4
#2I-Uen Hsu (UM: University of Michigan)H-Index: 2
Last. John Y. Kuwada (UM: University of Michigan)H-Index: 39
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#1Xiaofei Cong (VT: Virginia Tech)H-Index: 2
#2Jonathan Doering (VT: Virginia Tech)H-Index: 3
Last. Honglin Jiang (VT: Virginia Tech)H-Index: 22
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Background The SH3 and cysteine-rich domain 3 (Stac3) gene is specifically expressed in the skeletal muscle. Stac3 knockout mice die perinatally. In this study, we determined the potential role of Stac3 in postnatal skeletal muscle growth, fiber composition, and contraction by generating conditional Stac3 knockout mice.
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#1Alexander Polster (Anschutz Medical Campus)H-Index: 6
#2Benjamin R. Nelson (UTSW: University of Texas Southwestern Medical Center)H-Index: 8
Last. Kurt G. Beam (Anschutz Medical Campus)H-Index: 50
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Abstract In skeletal muscle, conformational coupling between CaV1.1 in the plasma membrane and type 1 ryanodine receptor (RyR1) in the sarcoplasmic reticulum (SR) is thought to underlie both excitation–contraction (EC) coupling Ca2+ release from the SR and retrograde coupling by which RyR1 increases the magnitude of the Ca2+ current via CaV1.1. Recent work has shown that EC coupling fails in muscle from mice and fish null for the protein Stac3 (SH3 and cysteine-rich domain 3) but did not establi...
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Summary STAC3 is a soluble protein essential for skeletal muscle excitation-contraction (EC) coupling. Through its tandem SH3 domains, it interacts with the cytosolic II-III loop of the skeletal muscle voltage-gated calcium channel. STAC3 is the target for a mutation (W284S) that causes Native American myopathy, but multiple other sequence variants have been reported. Here, we report a crystal structure of the human STAC3 tandem SH3 domains. We analyzed the effect of five disease-associated vari...
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#1Dmitry Shishmarev (ANU: Australian National University)H-Index: 7
Excitation-contraction coupling (ECC) is a physiological process that links excitation of muscles by the nervous system to their mechanical contraction. In skeletal muscle, ECC is initiated with an action potential, generated by the somatic nervous system, which causes a depolarisation of the muscle fibre membrane (sarcolemma). This leads to a rapid change in the transmembrane potential, which is detected by the voltage-gated Ca2+ channel dihydropyridine receptor (DHPR) embedded in the sarcolemm...
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Abstract Excitation-contraction coupling is the signaling process by which action potentials control calcium release and consequently the force of muscle contraction. Until recently, three triad proteins were known to be essential for skeletal muscle EC coupling: the voltage-gated calcium channel CaV1.1 acting as voltage sensor, the SR calcium release channel RyR1 representing the only relevant calcium source, and the auxiliary CaV β1a subunit. Whether CaV1.1 and RyR1 are directly coupled or whe...
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#2Edson Assunção Mareco (UWO: University of Western Ontario)H-Index: 3
Last. D. Garcia de la serrana (St And: University of St Andrews)H-Index: 1
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Abstract Fish size is a complex trait determined by the interaction of environmental and genetic factors. While evidence exists that fish final length and size are partially determined by muscle fibre structure. However, the molecular basis behind final body size and muscle fibre composition remains yet to be fully understood. Here we use the fish model zebrafish (Danio rerio) to explore the molecular mechanisms involved in muscle fibre number, muscle growth and their role on animal size determi...
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