Literature DB >> 10036236

Plectin is a linker of intermediate filaments to Z-discs in skeletal muscle fibers.

T Hijikata1, T Murakami, M Imamura, N Fujimaki, H Ishikawa.   

Abstract

Plectin is a versatile linker protein which is associated with various types of cytoskeletal components and/or filaments including intermediate filaments, and its deficiency causes the disruption of myofibrils, or muscular dystrophy. To better understand the functional role of plectin in skeletal muscle fibers, we have examined the topological and structural relationships of plectin to intermediate filaments and Z-discs in rat diaphragm muscles by confocal and immunoelectron microscopy. Immunofluorescence analysis revealed that plectin was colocalized with desmin at the periphery of Z-discs. This plectin localization around Z-discs was constantly maintained irrespective of the contracted or extended state of the muscle fibers, suggesting either direct or indirect association of plectin with Z-discs. Immunogold labeling in skinned muscle fibers clearly demonstrated that plectin-labeled fine threads linked desmin intermediate filaments to Z-discs and connected intermediate filaments to each other. These results indicate that through plectin threads desmin intermediate filaments form lateral linkages among adjacent Z-discs, preventing individual myofibrils from disruptive contraction and ensuring effective force generation.

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Year:  1999        PMID: 10036236     DOI: 10.1242/jcs.112.6.867

Source DB:  PubMed          Journal:  J Cell Sci        ISSN: 0021-9533            Impact factor:   5.285


  11 in total

1.  Desmuslin, an intermediate filament protein that interacts with alpha -dystrobrevin and desmin.

Authors:  Y Mizuno; T G Thompson; J R Guyon; H G Lidov; M Brosius; M Imamura; E Ozawa; S C Watkins; L M Kunkel
Journal:  Proc Natl Acad Sci U S A       Date:  2001-05-15       Impact factor: 11.205

2.  A compound heterozygous one amino-acid insertion/nonsense mutation in the plectin gene causes epidermolysis bullosa simplex with plectin deficiency.

Authors:  J W Bauer; F Rouan; B Kofler; G A Rezniczek; I Kornacker; W Muss; R Hametner; A Klausegger; A Huber; G Pohla-Gubo; G Wiche; J Uitto; H Hintner
Journal:  Am J Pathol       Date:  2001-02       Impact factor: 4.307

3.  Filamentous structures in skeletal muscle: anchors for the subsarcolemmal space.

Authors:  Astrid Feinisa Khairani; Yuki Tajika; Maiko Takahashi; Hitoshi Ueno; Tohru Murakami; Arifin Soenggono; Hiroshi Yorifuji
Journal:  Med Mol Morphol       Date:  2014-02-12       Impact factor: 2.309

4.  Plectin isoforms as organizers of intermediate filament cytoarchitecture.

Authors:  Gerhard Wiche; Lilli Winter
Journal:  Bioarchitecture       Date:  2011-01

5.  Plectin tethers desmin intermediate filaments onto subsarcolemmal dense plaques containing dystrophin and vinculin.

Authors:  Takao Hijikata; Tohru Murakami; Harunori Ishikawa; Hiroshi Yorifuji
Journal:  Histochem Cell Biol       Date:  2003-01-18       Impact factor: 4.304

6.  Obscurin-like 1, OBSL1, is a novel cytoskeletal protein related to obscurin.

Authors:  Sarah B Geisler; Dustin Robinson; Maria Hauringa; Maide O Raeker; Andrei B Borisov; Margaret V Westfall; Mark W Russell
Journal:  Genomics       Date:  2007-02-06       Impact factor: 5.736

Review 7.  Plectin-intermediate filament partnership in skin, skeletal muscle, and peripheral nerve.

Authors:  Maria J Castañón; Gernot Walko; Lilli Winter; Gerhard Wiche
Journal:  Histochem Cell Biol       Date:  2013-06-09       Impact factor: 4.304

8.  Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function.

Authors:  D J Milner; M Mavroidis; N Weisleder; Y Capetanaki
Journal:  J Cell Biol       Date:  2000-09-18       Impact factor: 10.539

9.  Genomic organization and single-nucleotide polymorphism map of desmuslin, a novel intermediate filament protein on chromosome 15q26.3.

Authors:  Y Mizuno; A A Puca; K F O'Brien; A H Beggs; L M Kunkel
Journal:  BMC Genet       Date:  2001-06-20       Impact factor: 2.797

10.  Myofiber integrity depends on desmin network targeting to Z-disks and costameres via distinct plectin isoforms.

Authors:  Patryk Konieczny; Peter Fuchs; Siegfried Reipert; Wolfram S Kunz; Anikó Zeöld; Irmgard Fischer; Denise Paulin; Rolf Schröder; Gerhard Wiche
Journal:  J Cell Biol       Date:  2008-05-19       Impact factor: 10.539

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