ArticleBiology open2014
Phospho-regulated Drosophila adducin is a determinant of synaptic plasticity in a complex with Dlg and PIP2 at the larval neuromuscular junction.
Article in Biology open, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- Methods to Study the Role of Cytoskeletal Motor Proteins in the Organization of the Postsynaptic Membrane.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Dynein-driven regulation of postsynaptic membrane architecture and synaptic function.Journal of cell science · 2025Article
- Muscle cofilin alters neuromuscular junction postsynaptic development to strengthen functional neurotransmission.Development (Cambridge, England) · 2024Article
- Synapse development and maturation at the drosophila neuromuscular junction.Neural development · 2020Review
- The conserved microRNA miR-34 regulates synaptogenesis via coordination of distinct mechanisms in presynaptic and postsynaptic cells.Nature communications · 2020Article
- Homeodomain-interacting protein kinase (Hipk) plays roles in nervous system and muscle structure and function.PloS one · 2020Article
- Article
- Tenectin recruits integrin to stabilize bouton architecture and regulate vesicle release at theeLife · 2018Article
- The Long 3'UTR mRNA ofThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2017Article
- Adducin at the Neuromuscular Junction in Amyotrophic Lateral Sclerosis: Hanging on for Dear Life.Frontiers in cellular neuroscience · 2016Review
- Detection of in situ protein-protein complexes at the Drosophila larval neuromuscular junction using proximity ligation assay.Journal of visualized experiments : JoVE · 2015Article
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Adducin is a ubiquitously expressed actin- and spectrin-binding protein involved in cytoskeleton organization, and is regulated through phosphorylation of the myristoylated alanine-rich C-terminal kinase (MARCKS)-homology domain by protein kinase C (PKC). We have previously shown that the Drosophila adducin, Hu-li tai shao (Hts), plays a role in larval neuromuscular junction (NMJ) growth. Here, we find that the predominant isoforms of Hts at the NMJ contain the MARCKS-homology domain, which is important for interactions with Discs large (Dlg) and phosphatidylinositol 4,5-bisphosphate (PIP2). Through the use of Proximity Ligation Assay (PLA), we show that the adducin-like Hts isoforms are in complexes with Dlg and PIP2 at the NMJ. We provide evidence that Hts promotes the phosphorylation and delocalization of Dlg at the NMJ through regulation of the transcript distribution of the PAR-1 and CaMKII kinases in the muscle. We also show that Hts interactions with Dlg and PIP2 are impeded through phosphorylation of the MARCKS-homology domain. These results are further evidence that Hts is a signaling-responsive regulator of synaptic plasticity in Drosophila.
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