ArticleHistochemistry and cell biology2003
Plectin tethers desmin intermediate filaments onto subsarcolemmal dense plaques containing dystrophin and vinculin.
Article in Histochemistry and cell biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 47 citations in OpenAlex.
- What does desmin do: A bibliometric assessment of the functions of the muscle intermediate filament.Experimental biology and medicine (Maywood, N.J.) · 2022Article
- Plectin in Skin Fragility Disorders.Cells · 2021Review
- Review
- Keratin 18 is an integral part of the intermediate filament network in murine skeletal muscle.American journal of physiology. Cell physiology · 2020Article
- Intermediate Filaments and the Plasma Membrane.Cold Spring Harbor perspectives in biology · 2017Review
- New insights into the protein aggregation pathology in myotilinopathy by combined proteomic and immunolocalization analyses.Acta neuropathologica communications · 2016Article
- The biochemical and mass spectrometric profiling of the dystrophin complexome from skeletal muscle.Computational and structural biotechnology journal · 2016Review
- Filamentous structures in skeletal muscle: anchors for the subsarcolemmal space.Medical molecular morphology · 2015Article
- Plectin-intermediate filament partnership in skin, skeletal muscle, and peripheral nerve.Histochemistry and cell biology · 2013Review
- Sarcospan: a small protein with large potential for Duchenne muscular dystrophy.Skeletal muscle · 2013Article
- Sarcospan-dependent Akt activation is required for utrophin expression and muscle regeneration.The Journal of cell biology · 2012Article
- A dystroglycan/plectin scaffold mediates mechanical pathway bifurcation in lung epithelial cells.The Journal of biological chemistry · 2011Article
- Overexpression of Galgt2 reduces dystrophic pathology in the skeletal muscles of alpha sarcoglycan-deficient mice.The American journal of pathology · 2009Article
- Intermediate filaments in smooth muscle.American journal of physiology. Cell physiology · 2008Review
- Absence of keratin 19 in mice causes skeletal myopathy with mitochondrial and sarcolemmal reorganization.Journal of cell science · 2007Article
- Differentiation of cardiomyocytes requires functional serine residues within the amino-terminal domain of desmin.Differentiation; research in biological diversity · 2007Article
- Plectin 1f scaffolding at the sarcolemma of dystrophic (mdx) muscle fibers through multiple interactions with beta-dystroglycan.The Journal of cell biology · 2007Article
- Specific interaction of the actin-binding domain of dystrophin with intermediate filaments containing keratin 19.Molecular biology of the cell · 2005Article
- Innovative techniques and applications in histochemistry and cell biology.Histochemistry and cell biology · 2003Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plectin is a versatile cytoskeletal linker protein that preferentially localizes at interfaces between intermediate filaments and the plasma membrane in muscle, epithelial cells, and other tissues. Its deficiency causes muscular dystrophy with epidermolysis bullosa simplex. To better understand the functional roles of plectin beneath the sarcolemma of skeletal muscles and to gain some insights into the underlying mechanism of plectin-deficient muscular dystrophy, we studied in vivo structural and molecular relationships of plectin to subsarcolemmal cytoskeletal components, such as desmin, dystrophin, and vinculin, in rat skeletal muscles. Immunogold electron microscopy revealed that plectin fine threads tethered desmin intermediate filaments onto subsarcolemmal dense plaques overlying Z-lines and I-bands. These dense plaques were found to contain dystrophin and vinculin, and thus may be the structural basis of costameres. The in vivo association of plectin with desmin, (meta-)vinculin, dystrophin, and actin was demonstrated by immunoprecipitation experiments. Treatment of plectin immunoprecipitates with gelsolin reduced actin, dystrophin, and (meta-)vinculin but not desmin, implicating that subsarcolemmal actin could partly mediate the interaction between plectin and dystrophin or (meta-)vinculin. Altogether, our data suggest that plectin, along with desmin intermediate filaments, might serve a vital structural role in the stabilization of the subsarcolemmal cytoskeleton.
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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.