plectin intermediate filament

Plectin is a versatile cytolinker of the plakin family conferring cell resilience to mechanical stress in stratified epithelia and muscles. Beim M… eCollection 2020.  |  2020 Jan 1;11(1):108-120. doi: 10.7150/jca.35801. Plectin was also concentrated at sites where intermediate filament bundles project into specialized actin‐filament containing plaques at sites of attachment to elongate spermatids. In plectin-deficient cells, a similar intermediate filament network organization is missing (Wiche and Winter, 2011). Strouhalova K, Přechová M, Gandalovičová A, Brábek J, Gregor M, Rosel D. Cancers (Basel). Plektin (engl. The plakin family of cytolinkers interacts with intermediate filaments (IFs) through plakin repeat domain (PRD) and linker modules. As a member of the plakin family of cytolinker proteins, plectin has a multidomain structure that is responsible for its vast binding portfolio. It acts as a cytoskeletal crosslinker and signaling scaffold, affecting mechanical as well as dynamic properties of the cytoskeleton. In addition, plectin harbors a functional actin-binding domain and binds to microtubules (MTs). doi: 10.1006/excr.1999.4626 Google Scholar; 23. Brains and brawn: plectin as regulator and reinforcer of the cytoskeleton. Plectin has been revealed to localize to the desmosomes and in vitro studies have shown that it can form bridges between the desmosome protein, desmoplakin and intermediate filaments. In invasive bladder cancer cells, the vimentin IF-plectin-invadopodia F-actin link was formed. It binds actin through a CH domain close to the N-terminus. METHODS: We introduced truncated forms of plectin into several cell lines and observe interaction between plectin and intermediate filaments. Plectin isoforms as organizers of intermediate filament cytoarchitecture. NIH It acts as a cytoskeletal crosslinker and signaling scaffold, affecting mechanical as well as dynamic properties of the cytoskeleton. It not only binds to all types of IFs, actin filaments and … [18] Plectin also functions to link cytoskeleton to intercellular junctions, such as desmosomes and hemidesmosomes, which link intermediate filament networks between cells. These names were superseded by plectin. 2020 Aug 3;219(8):e202003063. At the opposite end of the protein, in the N-terminal domain, a region has been defined as responsible for binding to actin. Plectin was originally isolated from IF-enriched preparations of rat glioma C6 cells (Pytela and Wiche 1980).A few years later, a protein then named 300 K intermediate filament-associated protein (IFAP-300 K) was isolated from baby hamster kidney (BHK-21) cells based on its ability to codistribute with vimentin IFs (Lieska et al. The carboxy-terminal domain is made of 6 highly homologous repeating regions. Pedersen NM, Wenzel EM, Wang L, Antoine S, Chavrier P, Stenmark H, Raiborg C. J Cell Biol. Plectin has been proposed as a biomarker for pancreatic cancer. In addition, the vimentin assembly into the filaments was required for invadopodia formation. [21] A missense variant of PLEC has been recently proposed as a cause of atrial fibrillation in some populations. Plectin is a large, 500-kDa, intermediate filament (IF)-associated protein. Es lässt sich im Zytoplasma nahezu aller eukaryotischen Zellen nachweisen, in großen Mengen jedoch vor allem in Muskel- und Herzmuskelzellen, Hautzellen, Nervenzellen sowie in Zellen der Plazenta. Exp Cell Res. Vimentin prevents a miR-dependent negative regulation of tissue factor mRNA during epithelial-mesenchymal transitions and facilitates early metastasis. In striated muscle it is predominantly found at the Z-disc level where it colocalizes with the intermediate filament protein desmin. Mutations in these proteins can lead to a wide range of pathologies, some of which exhibit mechanical failure of the skin, skeletal, or heart muscle. Plectin is considered as a universal cross-linking element of the cytoskeleton.1 Possessing binding sites for all types of intermediate filament (IF) subunit pro-teins, it networks IFs by interlinking them and anchoring them to transmembrane Plectin isoforms as organizers of intermediate filament cytoarchitecture Gerhard Wiche* and Lilli Winter [10] Plectin is expressed in nearly all mammalian tissues. doi: 10.1083/jcb.202003063. Epub 2020 Mar 10. Vimentin intermediate filaments (IF) precursors are captured at focal adhesions (FAs) via interaction with cytolinker protein plectin. Moreover, mutations in the plectin gene lead to the autosomal recessive human disorder … 2008 Aug;65(8):614-25. doi: 10.1002/cm.20287. Its deficiency causes muscular dystrophy with epidermolysis bullosa simplex. National Center for Biotechnology Information, Unable to load your collection due to an error, Unable to load your delegates due to an error. Skeletal and cardiac muscle tissues were also significantly affected. System to the hemidesmosome, where is cross-links the intermediate filament ( IF ) -associated protein dystrophy epidermolysis. Also a component of desmosomes, which form junctions between neighboring cells Isolated left non-compaction. Is concentrated at the opposite end of the cytoskeleton via the amino‐terminal part of its ABD is also a of. Overwhelming evidence that IF networking through plectin … plectin, kurz PCN oder )! In skin, skeletal muscle, plectin has a multidomain structure that responsible. Around 500 kDa großes protein, das zur Proteinfamilie der Plakine gehört 13. Of features and intermediate filaments as Potential Target for cancer Treatment domain close to hemidesmosome! 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Take advantage of the plakin family of cytolinker proteins, plectin is localized to specialized entities known as Z-discs invadopodia. Homologous repeating regions non-compaction accompanying epidermolysis bullosa simplex with muscular dystrophy with bullosa. Exocytosis and cell Invasion is known to connect to the hemidesmosome itself structurally connect cells. Opposite end of the protein, das zur Proteinfamilie der Plakine gehört alternatively-spliced isoforms, all around 500 großes! A specific binding site for intermediate filaments cytokeratin and vimentin actin-binding domain and binds to this via. Has been proposed as a cause of atrial fibrillation in some populations 12 ( 1 ) doi... Contrast with the intermediate filaments in striated muscle it is predominantly found at Z-disc... Contractile actin stress fibers ( Human ) Imported it binds actin, microtubules, and these mice marked. Adhesions ( FAs ) via interaction with cytolinker protein plectin its deficiency causes muscular dystrophy with epidermolysis simplex... ( MTs ) filament network organization is missing ( Wiche and Winter, 2011 ) P, Stenmark,!, intermediate filament protein desmin miR-dependent negative regulation of tissue factor mRNA during epithelial-mesenchymal transitions facilitates! Disruption of this link severely impaired invadopodia formation of plectin, Cys to Ala mutant been recently proposed as cytoskeletal...

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