ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2012
A role for the calmodulin kinase II-related anchoring protein (αkap) in maintaining the stability of nicotinic acetylcholine receptors.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Integrated Omics analysis of pig muscle metabolism under the effects of dietary Chlorella vulgaris and exogenous enzymes.Scientific reports · 2022Article
- Distinct roles of the dystrophin-glycoprotein complex: α-dystrobrevin and α-syntrophin in the maintenance of the postsynaptic apparatus of the neuromuscular synapse.Human molecular genetics · 2022Article
- The Metabolic Stability of the Nicotinic Acetylcholine Receptor at the Neuromuscular Junction.Cells · 2021Review
- Effects of nicotine on DARPP-32 and CaMKII signaling relevant to addiction.Advances in pharmacology (San Diego, Calif.) · 2021Review
- Phosphorylation of α-dystrobrevin is essential for αkap accumulation and acetylcholine receptor stability.The Journal of biological chemistry · 2020Article
- Evidence for the subsynaptic zone as a preferential site for CHRN recycling at neuromuscular junctions.Small GTPases · 2019Article
- Motor Endplate-Anatomical, Functional, and Molecular Concepts in the Historical Perspective.Cells · 2019Article
- Liprin-α-1 is a novel component of the murine neuromuscular junction and is involved in the organization of the postsynaptic machinery.Scientific reports · 2017Article
- Failure of lysosome clustering and positioning in the juxtanuclear region in cells deficient in rapsyn.Journal of cell science · 2015Article
- The knockdown of αkap alters the postsynaptic apparatus of neuromuscular junctions in living mice.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
- Role of autophagy, SQSTM1, SH3GLB1, and TRIM63 in the turnover of nicotinic acetylcholine receptors.Autophagy · 2014Article
- Degeneration of neuromuscular junction in age and dystrophy.Frontiers in aging neuroscience · 2014Review
- Exploring the nicotinic acetylcholine receptor-associated proteome with iTRAQ and transgenic mice.Genomics, proteomics & bioinformatics · 2013Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
αkap, a muscle specific anchoring protein encoded within the Camk2a gene, is thought to play a role in targeting multiple calcium/calmodulin kinase II isoforms to specific subcellular locations. Here we demonstrate a novel function of αkap in stabilizing nicotinic acetylcholine receptors (AChRs). Knockdown of αkap expression with shRNA significantly enhanced the degradation of AChR α-subunits (AChRα), leading to fewer and smaller AChR clusters on the surface of differentiated C2C12 myotubes. Mutagenesis and biochemical studies in HEK293T cells revealed that αkap promoted AChRα stability by a ubiquitin-dependent mechanism. In the absence of αkap, AChRα was heavily ubiquitinated, and the number of AChRα was increased by proteasome inhibitors. However, in the presence of αkap, AChRα was less ubiquitinated and proteasome inhibitors had almost no effect on AChRα accumulation. The major sites of AChRα ubiquitination reside within the large intracellular loop and mutations of critical lysine residues in this loop to arginine increased AChRα stability in the absence of αkap. These results provide an unexpected mechanism by which αkap controls receptor trafficking onto the surface of muscle cells and thus the maintenance of postsynaptic receptor density and synaptic function.
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