ArticleProceedings of the National Academy of Sciences of the United States of America2013
Domain cooperativity in the β1a subunit is essential for dihydropyridine receptor voltage sensing in skeletal muscle.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Interactive Role of the DHPR βBiomolecules · 2025Article
- In situ structural insights into the excitation-contraction coupling mechanism of skeletal muscle.Science advances · 2024Article
- CaHandbook of experimental pharmacology · 2023Article
- The distal C terminus of the dihydropyridine receptor βProceedings of the National Academy of Sciences of the United States of America · 2022Article
- New Insights in CaVβ Subunits: Role in the Regulation of Gene Expression and Cellular Homeostasis.Frontiers in cell and developmental biology · 2022Review
- Skeletal muscle CaPflugers Archiv : European journal of physiology · 2020Review
- Excitation-contraction coupling in skeletal muscle: recent progress and unanswered questions.Biophysical reviews · 2020Review
- Voltage sensing mechanism in skeletal muscle excitation-contraction coupling: coming of age or midlife crisis?Skeletal muscle · 2018Review
- Functional and structural characterization of a novel malignant hyperthermia-susceptible variant of DHPR-βAmerican journal of physiology. Cell physiology · 2018Article
- Structural and biophysical analyses of the skeletal dihydropyridine receptor β subunit βThe Journal of biological chemistry · 2017Article
- Congenital myopathy results from misregulation of a muscle Ca2+ channel by mutant Stac3.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The mammalian skeletal muscle DHPR has larger CaCell calcium · 2017Article
- Fluorescence Resonance Energy Transfer-based Structural Analysis of the Dihydropyridine Receptor α1S Subunit Reveals Conformational Differences Induced by Binding of the β1a Subunit.The Journal of biological chemistry · 2016Article
- The role of auxiliary subunits for the functional diversity of voltage-gated calcium channels.Journal of cellular physiology · 2015Review
- A Polybasic Plasma Membrane Binding Motif in the I-II Linker Stabilizes Voltage-gated CaV1.2 Calcium Channel Function.The Journal of biological chemistry · 2015Article
- Rem uncouples excitation-contraction coupling in adult skeletal muscle fibers.The Journal of general physiology · 2015Article
- Physiological and pharmacological modulation of the embryonic skeletal muscle calcium channel splice variant CaV1.1e.Biophysical journal · 2015Article
- The molecular architecture of dihydropyrindine receptor/L-type Ca2+ channel complex.Scientific reports · 2015Article
- Regions of ryanodine receptors that influence activation by the dihydropyridine receptor β1a subunit.Skeletal muscle · 2015Article
- Amino acid residues 489-503 of dihydropyridine receptor (DHPR) β1a subunit are critical for structural communication between the skeletal muscle DHPR complex and type 1 ryanodine receptor.The Journal of biological chemistry · 2014Article
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4 authors.
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Abstract
The dihydropyridine receptor (DHPR) β1a subunit is crucial for enhancement of DHPR triad expression, assembly of DHPRs in tetrads, and elicitation of DHPRα1S charge movement--the three prerequisites of skeletal muscle excitation-contraction coupling. Despite the ability to fully target α1S into triadic junctions and tetradic arrays, the neuronal isoform β3 was unable to restore considerable charge movement (measure of α1S voltage sensing) upon expression in β1-null zebrafish relaxed myotubes, unlike the other three vertebrate β-isoforms (β1a, β2a, and β4). Thus, we used β3 for chimerization with β1a to investigate whether any of the five distinct molecular regions of β1a is dominantly involved in inducing the voltage-sensing function of α1S. Surprisingly, systematic domain swapping between β1a and β3 revealed a pivotal role of the src homology 3 (SH3) domain and C terminus of β1a in charge movement restoration. More interestingly, β1a SH3 domain and C terminus, when simultaneously engineered into β3 sequence background, were able to fully restore charge movement together with proper intracellular Ca(2+) release, suggesting cooperativity of these two domains in induction of the α1S voltage-sensing function in skeletal muscle excitation-contraction coupling. Furthermore, substitution of a proline by alanine in the putative SH3-binding polyproline motif in the proximal C terminus of β1a (also of β2a and β4) fully obstructed α1S charge movement. Consequently, we postulate a model according to which β subunits, probably via the SH3-C-terminal polyproline interaction, adapt a discrete conformation required to modify the α1S conformation apt for voltage sensing in skeletal muscle.
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