ArticleThe Journal of cell biology1999
A PDZ-containing scaffold related to the dystrophin complex at the basolateral membrane of epithelial cells.
Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 98 citations in OpenAlex.
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- Aquaporin-4 in Neuromyelitis Optica Spectrum Disorders: A Target of Autoimmunity in the Central Nervous System.Biomolecules · 2022Review
- Extracellular matrix: an important regulator of cell functions and skeletal muscle development.Cell & bioscience · 2021Review
- Article
- Syntrophins entangled in cytoskeletal meshwork: Helping to hold it all together.Cell proliferation · 2019Review
- Biochemical and Functional Interplay Between Ion Channels and the Components of the Dystrophin-Associated Glycoprotein Complex.The Journal of membrane biology · 2018Review
- Cellular polarity in aging: role of redox regulation and nutrition.Genes & nutrition · 2014Article
- Amphiphysin I but not dynamin I nor synaptojanin mRNA expression increased after repeated methamphetamine administration in the rat cerebrum and cerebellum.Journal of neural transmission (Vienna, Austria : 1996) · 2013Article
- Syntrophin proteins as Santa Claus: role(s) in cell signal transduction.Cellular and molecular life sciences : CMLS · 2013Review
- β2-syntrophin and Par-3 promote an apicobasal Rac activity gradient at cell-cell junctions by differentially regulating Tiam1 activity.Nature cell biology · 2012Article
- Polarization and myelination in myelinating glia.ISRN neurology · 2012Article
- β2-Syntrophin is a Cdk5 substrate that restrains the motility of insulin secretory granules.PloS one · 2010Article
- The alpha-syntrophin PH and PDZ domains scaffold acetylcholine receptors, utrophin, and neuronal nitric oxide synthase at the neuromuscular junction.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
- Profound human/mouse differences in alpha-dystrobrevin isoforms: a novel syntrophin-binding site and promoter missing in mouse and rat.BMC biology · 2009Article
- Dystroglycan and perlecan provide a basal cue required for epithelial polarity during energetic stress.Developmental cell · 2009Article
- Regulation of insulin granule turnover in pancreatic beta-cells by cleaved ICA512.The Journal of biological chemistry · 2008Article
- Blood pressure is regulated by an alpha1D-adrenergic receptor/dystrophin signalosome.The Journal of biological chemistry · 2008Article
- Article
- Viral-mediated gene therapy for the muscular dystrophies: successes, limitations and recent advances.Biochimica et biophysica acta · 2007Review
- TIP-1 has PDZ scaffold antagonist activity.Molecular biology of the cell · 2006Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Membrane scaffolding complexes are key features of many cell types, serving as specialized links between the extracellular matrix and the actin cytoskeleton. An important scaffold in skeletal muscle is the dystrophin-associated protein complex. One of the proteins bound directly to dystrophin is syntrophin, a modular protein comprised entirely of interaction motifs, including PDZ (protein domain named for PSD-95, discs large, ZO-1) and pleckstrin homology (PH) domains. In skeletal muscle, the syntrophin PDZ domain recruits sodium channels and signaling molecules, such as neuronal nitric oxide synthase, to the dystrophin complex. In epithelia, we identified a variation of the dystrophin complex, in which syntrophin, and the dystrophin homologues, utrophin and dystrobrevin, are restricted to the basolateral membrane. We used exogenously expressed green fluorescent protein (GFP)-tagged fusion proteins to determine which domains of syntrophin are responsible for its polarized localization. GFP-tagged full-length syntrophin targeted to the basolateral membrane, but individual domains remained in the cytoplasm. In contrast, the second PH domain tandemly linked to a highly conserved, COOH-terminal region was sufficient for basolateral membrane targeting and association with utrophin. The results suggest an interaction between syntrophin and utrophin that leaves the PDZ domain of syntrophin available to recruit additional proteins to the epithelial basolateral membrane. The assembly of multiprotein signaling complexes at sites of membrane specialization may be a widespread function of dystrophin-related protein complexes.
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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.