ArticleThe Journal of biological chemistry2011
Homodimerization of the Src homology 3 domain of the calcium channel β-subunit drives dynamin-dependent endocytosis.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed, 37 citations in OpenAlex.
- Molecular Partners of Voltage-Gated Calcium Channel β and αThe Journal of membrane biology · 2026Review
- Mapping the interaction surface between CaNature communications · 2025Article
- The membrane-associated β2e-subunit of voltage-gated calcium channels translocates to the nucleus and regulates gene expression.Frontiers in physiology · 2025Article
- Inhibitory effects on L- and N-type calcium channels by a novel CaNaunyn-Schmiedeberg's archives of pharmacology · 2022Article
- Crossroads between membrane trafficking machinery and copper homeostasis in the nerve system.Open biology · 2021Review
- The life cycle of voltage-gated CaNeuronal signaling · 2021Review
- Nanoenviroments of the β-Subunit of L-Type Voltage-Gated Calcium Channels in Adult Cardiomyocytes.Frontiers in cell and developmental biology · 2021Article
- The βFrontiers in cardiovascular medicine · 2021Article
- A Tripartite Interaction Among the Calcium Channel αFrontiers in cellular neuroscience · 2019Article
- Rapid Turnover of the Cardiac L-Type CaiScience · 2018Article
- Constitutive activity of the Ghrelin receptor reduces surface expression of voltage-gated CaJournal of cell science · 2017Article
- Structural and biophysical analyses of the skeletal dihydropyridine receptor β subunit βThe Journal of biological chemistry · 2017Article
- Direct interaction of CaVβ with actin up-regulates L-type calcium currents in HL-1 cardiomyocytes.The Journal of biological chemistry · 2015Article
- The Cavβ1a subunit regulates gene expression and suppresses myogenin in muscle progenitor cells.The Journal of cell biology · 2014Article
- Structure-function of proteins interacting with the α1 pore-forming subunit of high-voltage-activated calcium channels.Frontiers in physiology · 2014Review
- Structure and function of the β subunit of voltage-gated Ca²⁺ channels.Biochimica et biophysica acta · 2013Review
- A local, periactive zone endocytic machinery at photoreceptor synapses in close vicinity to synaptic ribbons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Quantitative intensity-based FRET approaches--a comparative snapshot.Biophysical journal · 2012Review
- A quartet of leucine residues in the guanylate kinase domain of CaVβ determines the plasma membrane density of the CaV2.3 channel.The Journal of biological chemistry · 2012Article
- A short polybasic segment between the two conserved domains of the β2a-subunit modulates the rate of inactivation of R-type calcium channel.The Journal of biological chemistry · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Voltage-dependent calcium channels constitute the main entry pathway for calcium into excitable cells. They are heteromultimers formed by an α(1) pore-forming subunit (Ca(V)α(1)) and accessory subunits. To achieve a precise coordination of calcium signals, the expression and activity of these channels is tightly controlled. The accessory β-subunit (Ca(V)β), a membrane associated guanylate kinase containing one guanylate kinase (β-GK) and one Src homology 3 (β-SH3) domain, has antagonistic effects on calcium currents by regulating different aspects of channel function. Although β-GK binds to a conserved site within the α(1)-pore-forming subunit and facilitates channel opening, β-SH3 binds to dynamin and promotes endocytosis. Here, we investigated the molecular switch underlying the functional duality of this modular protein. We show that β-SH3 homodimerizes through a single disulfide bond. Substitution of the only cysteine residue abolishes dimerization and impairs internalization of L-type Ca(V)1.2 channels expressed in Xenopus oocytes while preserving dynamin binding. Covalent linkage of the β-SH3 dimerization-deficient mutant yields a concatamer that binds to dynamin and restores endocytosis. Moreover, using FRET analysis, we show in living cells that Ca(V)β form oligomers and that this interaction is reduced by Ca(V)α(1). Association of Ca(V)β with a polypeptide encoding the binding motif in Ca(V)α(1) inhibited endocytosis. Together, these findings reveal that β-SH3 dimerization is crucial for endocytosis and suggest that channel activation and internalization are two mutually exclusive functions of Ca(V)β. We propose that a change in the oligomeric state of Ca(V)β is the functional switch between channel activator and channel internalizer.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.