Marta Campiglio
Innsbruck Medical University
Voltage-dependent calcium channelBiochemistryCalcium channelBiologyCell biology
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Publications 29
#1Britany Rufenach (UBC: University of British Columbia)
#2Darren Christy (UBC: University of British Columbia)H-Index: 1
Last. Filip Van Petegem (UBC: University of British Columbia)H-Index: 29
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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...
#2Leonie von Elsner (UHH: University of Hamburg)H-Index: 2
Last. Kerstin Kutsche (UHH: University of Hamburg)H-Index: 33
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P/Q-type channels are the principal presynaptic calcium channels in brain functioning in neurotransmitter release. They are composed of the pore-forming CaV2.1 α1 subunit and the auxiliary α2δ-2 and β4 subunits. β4 is encoded by CACNB4, and its multiple splice variants serve isoform-specific functions as channel subunits and transcriptional regulators in the nucleus. In two siblings with intellectual disability, psychomotor retardation, blindness, epilepsy, movement disorder and cerebellar atrop...
1 CitationsSource
#2Valentina Di Biase (Innsbruck Medical University)H-Index: 9
Last. Stefan WagnerH-Index: 48
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#1Yousra El GhalebH-Index: 1
Last. Bernhard E. FlucherH-Index: 37
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#2Stefanie GeislerH-Index: 20
Last. G. J. Obermair (UHSA: University of Health Sciences Antigua)
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In nerve cells the genes encoding for α2δ subunits of voltage-gated calcium channels (VGCCs) have been linked to synaptic functions and neurological disease. Here we show that α2δ subunits are essential for the formation and organization of glutamatergic synapses. Using a cellular α2δ subunit triple loss-of-function model, we demonstrate a failure in presynaptic differentiation associated with the downscaling of postsynaptic AMPA receptors and the postsynaptic density. The role of α2δ isoforms a...
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...
3 CitationsSource
Presynaptic α 2 δ subunits of voltage-gated calcium channels regulate channel abundance and are involved in glutamatergic synapse formation. However, little is known about the specific functions of the individual α 2 δ isoforms and their role in GABAergic synapses. Using primary neuronal cultures of embryonic mice of both sexes, we here report that presynaptic overexpression of α 2 δ-2 in GABAergic synapses strongly increases clustering of postsynaptic GABA A Rs. Strikingly, presynaptic α 2 δ-2 ...
5 CitationsSource
#1Yousra El GhalebH-Index: 1
#2Marta CampiglioH-Index: 10
Last. Bernhard E. FlucherH-Index: 37
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ABSTRACTThe voltage-gated calcium channel CaV1.1a primarily functions as voltage-sensor in skeletal muscle excitation-contraction (EC) coupling. In embryonic muscle the splice variant CaV1.1e, which lacks exon 29, additionally function as a genuine L-type calcium channel. Because previous work in most laboratories used a CaV1.1 expression plasmid containing a single amino acid substitution (R165K) of a critical gating charge in the first voltage-sensing domain (VSD), we corrected this substituti...
: 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 dom...
2 CitationsSource
#1Pierre Costé de Bagneaux (Innsbruck Medical University)H-Index: 3
#2Marta Campiglio (Innsbruck Medical University)H-Index: 10
Last. Bernhard E. Flucher (Innsbruck Medical University)H-Index: 37
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ABSTRACTVoltage-dependent calcium channels (CaV) activate over a wide range of membrane potentials, and the voltage-dependence of activation of specific channel isoforms is exquisitely tuned to their diverse functions in excitable cells. Alternative splicing further adds to the stunning diversity of gating properties. For example, developmentally regulated insertion of an alternatively spliced exon 29 in the fourth voltage-sensing domain (VSD IV) of CaV1.1 right-shifts voltage-dependence of acti...
3 CitationsSource