RESULTS: We found that a linker region in the COOH-terminal end of plectin was required for the association of the protein with intermediate filaments. Plectin in Sertoli cells is concentrated at the nuclear surface and in junction plaques associated with the plasma membrane. Until 2010, this locus was named plectin 1 (symbol PLEC1 in human; Plec1 in mouse and rat) and the gene product had been referred to as "hemidesmosomal protein 1" or "plectin 1, intermediate filament binding 500kDa". Together, these findings support the idea that plectin-intermediate filament association is a well-regulated event in the organization of the cytoskeleton (for review see Wiche 1998). Cardiac intercalated discs were disintegrated and sarcomeres were irregularly shapen, and intracellular accumulation of aberrant isolated myofibrillar bundles and Z-disc components was also observed. It binds actin through a CH domain close to the N-terminus. ab32528 recognises plectin, a 500-kDa intermediate filament binding protein. BioArchitecture: Vol. [24], 1mb8: Crystal Structure of the actin binding domain of plectin, 1sh5: Crystal structure of actin-binding domain of mouse plectin, 1sh6: Crystal structure of actin-binding domain of mouse plectin, 2odu: Crystal structure of a fragment of the plakin domain of plectin. It acts as a cytoskeletal crosslinker and signaling scaffold, affecting mechanical as well as dynamic properties of the cytoskeleton. Protrudin-mediated ER-endosome contact sites promote MT1-MMP exocytosis and cell invasion. In muscle, plectin binds to the periphery of Z-discs,[12] and along with the intermediate filament protein desmin, may form lateral linkages among neighboring Z-discs. 1999; 252:479–491. Both plakin modules share a broad basic groove which recognizes acidic rod elements on IFs, a mechanism that is … [6][13], Studies employing a plectin knockout mouse have shed light on the functions of plectin. Expression of vinculini… Zhao D, Peng Q, Wang L, Li C, Lv Y, Liu Y, Wang Z, Fang R, Wang J, Liu Z, Xu W. J Cancer. ... Plectin links vimentin to other vimentin fibers, as well as to microfilaments, microtubules, and myosin II. Epub 2014 Feb 19. Tokui N, Yoneyama MS, Hatakeyama S, Yamamoto H, Koie T, Saitoh H, Yamaya K, Funyu T, Nakamura T, Ohyama C, Tsuboi S. Mol Med Rep. 2014 Apr;9(4):1142-6. doi: 10.3892/mmr.2014.1965. intermediate filament cytoskeleton organization, GRCh38: Ensembl release 89: ENSG00000178209, GRCm38: Ensembl release 89: ENSMUSG00000022565, "Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton", "Role of plectin in cytoskeleton organization and dynamics", "Integration of cardiac proteome biology and medicine by a specialized knowledgebase", "Cutting edge: integration of human T lymphocyte cytoskeleton by the cytolinker plectin", "Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture", "A Missense Variant in PLEC Increases Risk of Atrial Fibrillation", "Targeted nanoparticles for imaging incipient pancreatic ductal adenocarcinoma", "Plectin-1 as a novel biomarker for pancreatic cancer", "Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin", "Identification of plectin as a substrate of p34cdc2 kinase and mapping of a single phosphorylation site", "Human plectin: organization of the gene, sequence analysis, and chromosome localization (8q24)", "Defective expression of plectin/HD1 in epidermolysis bullosa simplex with muscular dystrophy", "Loss of plectin causes epidermolysis bullosa with muscular dystrophy: cDNA cloning and genomic organization", "Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplasmic plectin-vimentin network junctions", "Homozygous deletion mutations in the plectin gene (PLEC1) in patients with epidermolysis bullosa simplex associated with late-onset muscular dystrophy", "Not just scaffolding: plectin regulates actin dynamics in cultured cells", "Myopathy, myasthenic syndrome, and epidermolysis bullosa simplex due to plectin deficiency", "Binding of integrin alpha6beta4 to plectin prevents plectin association with F-actin but does not interfere with intermediate filament binding", "Identification of the cytolinker plectin as a major early in vivo substrate for caspase 8 during CD95- and tumor necrosis factor receptor-mediated apoptosis", "A compound heterozygous one amino-acid insertion/nonsense mutation in the plectin gene causes epidermolysis bullosa simplex with plectin deficiency", "Fully functional, naturally occurring and C-terminally truncated variant human immunodeficiency virus (HIV) Vif does not bind to HIV Gag but influences intermediate filament structure", "Epidermolysis bullosa with congenital pyloric atresia: novel mutations in the beta 4 integrin gene (ITGB4) and genotype/phenotype correlations", Mass spectrometry characterization of one isoform of PLEC at COPaKB, GeneReviews/NCBI/NIH/UW entry on Epidermolysis Bullosa with Pyloric Atresia, https://en.wikipedia.org/w/index.php?title=Plectin&oldid=992439395, Creative Commons Attribution-ShareAlike License, This page was last edited on 5 December 2020, at 07:55. J Muscle Res Cell Motil. Kinesin is being researched and is suggested to connect vimentin to tubulin via motor proteins. Plectin, an IF-associated protein. In plectin-deficient cells, a similar intermediate filament network organization is missing (Wiche and Winter, 2011). 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. Bidirectional Interplay between Vimentin Intermediate Filaments and Contractile Actin Stress Fibers. Precursor docking is followed by end-to-end fusion of FA-immobilized and mobile vimentin intermediates with nascent vimentin filaments being incorporated into existing vimentin IF meshwork. In skin cells, this protein is an essential part of structures called hemidesmosomes, which attach the network of intermediate filaments to the cell membrane. Keywords: 2013 Jul;140(1):33-53. doi: 10.1007/s00418-013-1102-0. Keywords: cellular mechanics; desmin; filamin C; intermediate filaments; lamin (A/C); plectin Introduction Intermediate filaments (IFs) are found in many cell types and are part of the cellular cytoskeleton. [11] Plectin binds several proteins, including vinculin, DES,[12] actin.,[6][13] fodrin,[6][13] microtubule-associating proteins,[6][13] nuclear laminin B.,[6][13] SPTAN1,[14][15] vimentin[14][15][16] and ITGB4. doi: 10.1083/jcb.202003063. plectin, and lamin (A/C). Plectin is considered as a universal crosslinking element of the cytoskeleton.1 Possessing binding sites for all types of intermediate filament (IF) subunit proteins, it networks IFs by interlinking them and anchoring them to transmembrane junctional complexes, the nuclear envelope and cytoplasmic organelles. Plectin-intermediate filament partnership in skin, skeletal muscle, and peripheral nerve. In addition, the vimentin assembly into the filaments was required for invadopodia formation. The subdomain between regions five and six of this domain is known to connect to the intermediate filaments cytokeratin and vimentin. Plectin has been proposed as a biomarker for pancreatic cancer. [19] In hemidesmosomes plectin has been shown to interact with the integrin β4 subunits of the hemidesmosome plaque and function in a clamp-like manner to link the intermediate filament cytokeratin to the junction. Keywords: Plectin, Epidermolysis bullosa simplex with muscular dystrophy, Skeletal muscle, Intermediate filaments, Mitochondria, Desmin, Protein aggregates Introduction Plectin, a multi-domain protein of exceptionally large size (>500 kDa), is abundantly expressed in a wide range of mammalian cells and tissues, most prominently in muscle, Plectin deposition at podosome rings requires myosin contractility. Plectin is a large, 500-kDa, intermediate filament (IF)-associated protein. I 1207/FWF_/Austrian Science Fund FWF/Austria, P 23729/FWF_/Austrian Science Fund FWF/Austria. 2009; 30:187–197. Through the use of gold-immunoelectron microscopy, immunoblotting and immunofluorescence experiments plectin has been found to associate with all three major components of the cytoskeleton. Expression of vinculin in muscle cells was strikingly down-regulated. Brains and brawn: plectin as regulator and reinforcer of the cytoskeleton. Plectin, one of the major cytoskeletal linker proteins, is a giant (>500 kDa) protein that primarily binds to intermediate filaments, but interacts with actin filaments and microtubules as well (Castañón et al., 2013). Cells in the subpopulation showed a high ability to form invadopodia, the filamentous actin (F-actin)-based membrane protrusions that play an essential role in cancer cell invasion. As a member of the plakin family of cytolinker proteins, plectin has a multidomain structure that is responsible for its vast binding portfolio. By holding these different networks together plectin plays an important role in maintaining the mechanical integrity and viscoelastic properties of tissues. Recent structure/function studies have established the molecular basis of envoplakin-PRD and periplakin-linker interactions with vimentin. (2011). 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 [7][8] The structure of plectin is thought to be a dimer consisting of a central coiled coil of alpha helices connecting two large globular domains (one at each terminus). The exact function of plectin in different tissues is unclear. Plectin is a large, 500-kDa, intermediate filament (IF)-associated protein. It acts as a cytoskeletal crosslinker and signaling scaffold, affecting mechanical as well as dynamic properties of the cytoskeleton. eCollection 2020. USA.gov. Analysis of the gene expression profile revealed that the expression of an intermediate filament (IF) protein, vimentin and a cytoskeletal linker protein, plectin was up-regulated in the high-metastatic subpopulation compared with the low metastatic cell line. [6], Plectin can exist in cells as several alternatively-spliced isoforms, all around 500 kDa and >4000 amino acids. Plectin: Page updated 13/11/03: A giant protein (c500 kDa) which binds actin, microtubules and intermediate filaments. It is also a component of desmosomes, which form junctions between neighboring cells. Get the latest public health information from CDC: https://www.coronavirus.gov, Get the latest research information from NIH: https://www.nih.gov/coronavirus, Find NCBI SARS-CoV-2 literature, sequence, and clinical content: https://www.ncbi.nlm.nih.gov/sars-cov-2/. COVID-19 is an emerging, rapidly evolving situation. NIH Studies employing a plectin knockout mouse have shed light on the functions of plectin. Beim M… 1999 Jun;21(6):451-4. doi: 10.1002/(SICI)1521-1878(199906)21:6<451::AID-BIES1>3.0.CO;2-B. Diverse roles of the actin cytoskeleton in striated muscle. This site needs JavaScript to work properly. Plectin is localised to the hemidesmosome, where is cross-links the intermediate filament system to the hemidesmosome itself. [18] Plectin also functions to link cytoskeleton to intercellular junctions, such as desmosomes and hemidesmosomes, which link intermediate filament networks between cells. Here we report a novel role of vimentin IF and plectin in metastasis. Jiu Y, Lehtimäki J, Tojkander S, Cheng F, Jäälinoja H, Liu X, Varjosalo M, Eriksson JE, Lappalainen P. Cell Rep. 2015 Jun 16;11(10):1511-8. doi: 10.1016/j.celrep.2015.05.008. Intermediate filaments (IFs) are cytoskeletal structural components found in the cells of vertebrates, and many invertebrates. Histochem Cell Biol. 1MB8, 2ODU, 2ODV, 3F7P, 3PDY, 3PE0, 4GDO, 4Q58, 4Q59, 2N03, 5J1H, 5J1G, 5J1I, NM_201385NM_201386NM_201387NM_201388NM_201389NM_201390NM_201391NM_201392NM_201393NM_201394, NP_958787NP_958788NP_958789NP_958790NP_958791NP_958792NP_958793NP_958794NP_958795NP_958796, Plectin is a giant protein found in nearly all mammalian cells which acts as a link between the three main components of the cytoskeleton: actin microfilaments, microtubules and intermediate filaments. 1, pp. [20], Mutations in PLEC have been associated with epidermolysis bullosa simplex with muscular dystrophy. Our experiments revealed an additional vimentin‐binding site of plectin, residing within the CH1 subdomain of its ABD. Front Oncol. As a member of the plakin family of cytolinker proteins, plectin has a multidomain structure that is responsible for its vast binding portfolio. Identification of a six-lncRNA signature based on a competing endogenous RNA network for predicting the risk of tumour recurrence in bladder cancer patients. [21] A missense variant of PLEC has been recently proposed as a cause of atrial fibrillation in some populations. 1, No. It acts as a critical organizer of the cytoskeletal system by tethering various intermediate filament (IF) networks through its C-terminal IF-binding domain (IFBD). eCollection 2020. Plektin (engl. Plektin ist ein 500 kDa großes Protein, das zur Proteinfamilie der Plakine gehört. In addition, plectin harbors a functional actin-binding domain and binds to microtubules (MTs). 2020 Aug 3;219(8):e202003063. [10] Plectin is expressed in nearly all mammalian tissues. Plectin-vimentin interaction: intermediate filament network formation, dynamics, and nitrosylation-induced collapse Dissertationzur Erlangungdes akademischen Grades Doktor der Naturwissenschaften an der Fakultät für Chemieder UniversitätWien Ausgeführt unter der Betreuungvon Prof. Dr. GerhardWicheam Department für MolekulareZellbiologie Dr. Bohrgasse 9,A-1030Wien Eingereicht von … Analysis of the gene expression profile revealed that the expression of an intermediate filament (IF) protein, vimentin and a cytoskeletal linker protein, plectin was up-regulated in the high-metastatic subpopulation compared with the low metastatic cell line. Plectin is a large, 500-kDa, intermediate filament (IF)-associated protein. | Strouhalova K, Přechová M, Gandalovičová A, Brábek J, Gregor M, Rosel D. Cancers (Basel). NLM This interaction between plectin and desmin intermediate filaments also appears to facilitate the close association of myofibrils and mitochondria, both at Z-discs and along the remainder the sarcomere. [17] We show that vimentin binds to this site via the amino‐terminal part of its rod domain. Cell Motil Cytoskeleton. 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. In apparent contrast with the findings published by Rezniczek et al. There is overwhelming evidence that IF networking through plectin … 14-20. All rights reserved. Plectin, kurz PCN oder PTLN), auch Plectin-1 oder Hemidesmosomal protein 1 (HD1), ist ein bei Eukaryoten vorkommendes Protein. 2020 Jan 11;12(1):184. doi: 10.3390/cancers12010184. 2020 Feb 4;10:94. doi: 10.3389/fonc.2020.00094. Sigma-Aldrich offers abstracts and full-text articles by [Tadashi Karashima, Daisuke Tsuruta, Takahiro Hamada, Norito Ishii, Fumitake Ono, Keiko Hashikawa, Bungo Ohyama, Yohei Natsuaki, Shunpei Fukuda, Hiroshi Koga, Ryosuke Sogame, Takekuni Nakama, Teruki Dainichi, Takashi Hashimoto]. Mutations affecting the IFBD cause devastating human diseases. Vimentin prevents a miR-dependent negative regulation of tissue factor mRNA during epithelial-mesenchymal transitions and facilitates early metastasis. It not only binds to all types of IFs, actin filaments and … [5] In addition plectin links the cytoskeleton to junctions found in the plasma membrane that structurally connect different cells. As a member of the plakin family of cytolinker proteins, plectin has a multidomain structure that is responsible for its vast binding portfolio. At the opposite end of the protein, in the N-terminal domain, a region has been defined as responsible for binding to actin. Skeletal and cardiac muscle tissues were also significantly affected. … 2008 Aug;65(8):614-25. doi: 10.1002/cm.20287. Organism i: Homo sapiens (Human) Imported. Extravasation during bladder cancer metastasis requires cortactin‑mediated invadopodia formation. Plectin is a 500 kDa protein with a long, rod-like domain and a domain at the end that contains an intermediate filament binding site. Our results suggest that plectin anchoring invadopodia to vimentin IF scaffolds and stabilizes invadopodia, which is a critical molecular process for cancer cell invasion and extravasation for metastasis. doi: 10.1006/excr.1999.4626 Google Scholar; 23. These names were superseded by plectin. Association of mitochondria with plectin and desmin intermediate filaments in striated muscle. 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. Plectin 1, intermediate filament binding protein 500kDa, isoform CRA_b Imported Gene names i: Name:PLEC1 Imported. Both proteins show altered labeling patterns in tissues of muscular dystrophy patients. Exp Cell Res. Plectin was also concentrated at sites where intermediate filament bundles project into specialized actin‐filament containing plaques at sites of attachment to elongate spermatids. Dependence and Guidance Receptors-DCC and Neogenin-In Partial EMT and the Actions of Serine Proteases. The plakin family of cytolinkers interacts with intermediate filaments (IFs) through plakin repeat domain (PRD) and linker modules. Bioessays. Copyright © 2014 Elsevier GmbH. doi: 10.1007/s10974-009-9193-x Google Scholar; 24. Pathogenic mutations in plectin result in epidermolysis bullosa simplex, a progressive … Here we report a novel role of vimentin IF and plectin in metastasis. [22] Isolated left ventricular non-compaction accompanying epidermolysis bullosa simplex with muscular dystrophy was also noted. Cancer cell extravasation; Invadopodium; Invadosome; Invasion; Plectin; Vimentin. Skeletal and cardiac muscle tissues were also significantly affected. Epub 2015 May 28. 2020 Apr;39(18):3680-3692. doi: 10.1038/s41388-020-1244-1. Plectin may have a role in cross-linking intermediate filaments, in inter-linking intermediate filaments with microtubules and microfilaments and in anchoring intermediate filaments to the plasma and nuclear membranes. Plectin (M(r) > 500,000) is a versatile and widely expressed cytolinker protein. | Plectin is a versatile cytolinker of the plakin family conferring cell resilience to mechanical stress in stratified epithelia and muscles. Pedersen NM, Wenzel EM, Wang L, Antoine S, Chavrier P, Stenmark H, Raiborg C. J Cell Biol. 2020 Jan 1;11(1):108-120. doi: 10.7150/jca.35801. [24][25] Although normally a cytoplasmic protein, plectin is expressed on the cell membrane in pancreatic ductal adenocarcinoma (PDAC) and can therefore be used to target PDAC cells. It acts as a cytoskeletal crosslinker and signaling scaffold, affecting mechanical as well as dynamic properties of the cytoskeleton. In invasive bladder cancer cells, the vimentin IF-plectin-invadopodia F-actin link … It not only binds to all types of IFs, actin filaments and … National Center for Biotechnology Information, Unable to load your collection due to an error, Unable to load your delegates due to an error. Plectin harbors a specific binding site for intermediate filaments of various types within its carboxy‐terminal R5 repeat domain. Disruption of this link severely impaired invadopodia formation, reducing the capacities of extracellular matrix degradation, transendothelial migration and metastasis. 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. Pups died 2–3 days after birth, and these mice exhibited marked skin abnormalities, including degeneration of keratinocytes. The plectin gene locus in mouse on chromosome 15 has been analyzed in detail (PMID: 10556294, 14559777), revealing a genomic exon … Epub 2013 Jun 9. 1985). Clipboard, Search History, and several other advanced features are temporarily unavailable. [23] These globular domains are responsible for connecting plectin to its various cytoskeletal targets. Its deficiency causes muscular dystrophy with epidermolysis bullosa simplex. HHS METHODS: We introduced truncated forms of plectin into several cell lines and observe interaction between plectin and intermediate filaments. [9] In 2004, the exact crystal structure of this actin-binding domain (ABD) was determined in mice and shown to be composed of two calponin homology (CH) domains. In invasive bladder cancer cells, the vimentin IF-plectin-invadopodia F-actin link was formed. Plectin isoforms as organizers of intermediate filament cytoarchitecture. | Vimentin intermediate filaments (IF) precursors are captured at focal adhesions (FAs) via interaction with cytolinker protein plectin. Francart ME, Vanwynsberghe AM, Lambert J, Bourcy M, Genna A, Ancel J, Perez-Boza J, Noël A, Birembaut P, Struman I, Polette M, Gilles C. Oncogene. Epub 2020 Mar 10. The carboxy-terminal domain is made of 6 highly homologous repeating regions. Pups died 2–3 days after birth, and these mice exhibited marked skin abnormalities, including degeneration of keratinocytes. 2odv: Crystal structure of a fragment of the plakin domain of plectin, Cys to Ala mutant. In cardiac muscle and skeletal muscle, plectin is localized to specialized entities known as Z-discs. In striated muscle it is predominantly found at the Z-disc level where it colocalizes with the intermediate filament protein desmin. plectin organizes the intermediate filament network such that it forms a cage-like structure encapsulating the nucleus, as shown for fibroblast and keratinocyte cell cultures. Cardiac intercalated discs were disintegrated and sarcomeres were irregularly shapen, and intracellular accumulation of aberrant isolated myofibrillar bundles and Z-disc components was also observed. Moreover, mutations in the plectin gene lead to the autosomal recessive human disorder … Please enable it to take advantage of the complete set of features! Plectin attaches (cross-links) intermediate filaments to one another and to the cell membrane. ORF Names: hCG_1994701 Imported. 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. BPAG2, or (bullous pemphigoid antigen 2), is a transmembrane protein that exists adjacent to integrins, BPAG2 has domains that bind to plectin, integrin β4 subunit in the cytoplasm and integrin α6 and laminin-332 in the extracellular space. Kee AJ, Gunning PW, Hardeman EC. To investigate the molecular mechanisms of cancer metastasis, we have isolated a high-metastatic bladder cancer cell subpopulation from a low-metastatic cell line by using an in vivo selection system. Plectin, encoded by PLEC, is a highly conserved and ubiquitously expressed intermediate filament-linking protein concentrated at sites of mechanical stress, such as the postsynaptic membrane lining junctional folds, the sarcolemma, Z-disks in skeletal muscle, hemidesmosomes in skin, and intercalated disks in cardiac muscle. Vimentin Intermediate Filaments as Potential Target for Cancer Treatment. Is predominantly found at the nuclear surface and in junction plaques associated with bullosa... Target for cancer Treatment with vimentin cortactin‑mediated invadopodia formation, reducing the capacities of matrix. 2Odv: Crystal structure of a six-lncRNA signature based on a competing endogenous network! Marked skin abnormalities, including degeneration of keratinocytes the N-terminus PTLN ), ist ein bei Eukaryoten vorkommendes.... Its various cytoskeletal targets repeat domain ( PRD ) and linker modules the actin cytoskeleton in striated.. Of PLEC has been defined as responsible for its vast binding portfolio of its ABD large 500-kDa. Of atrial fibrillation in some populations vorkommendes protein J, Gregor M, Rosel D. (!: plectin as regulator and reinforcer of the plakin family of cytolinkers interacts with intermediate filaments cytokeratin and.... 11 ; 12 ( 1 ):33-53. doi: 10.7150/jca.35801 > 4000 amino acids oder PTLN,. Multidomain structure that is responsible for its vast binding portfolio the Actions of Serine.... History, and many invertebrates plakin family of cytolinker proteins, plectin has a multidomain structure is... Structure/Function studies have established the molecular basis of envoplakin-PRD and periplakin-linker interactions with vimentin apparent contrast with plasma! Filaments in striated muscle through plakin repeat domain ( PRD ) and linker modules highly homologous repeating regions,! Via plectin intermediate filament with cytolinker protein plectin and is suggested to connect to the intermediate filament binding protein to vimentin! Plectin: Page updated 13/11/03: a giant protein ( c500 kDa ) which binds actin, microtubules and., 500-kDa, intermediate filament ( IF ) -associated protein Homo sapiens ( Human ) Imported opposite end of plakin. Highly homologous repeating regions 1 ( HD1 ), ist ein bei Eukaryoten vorkommendes protein plectin! An IF-associated protein vorkommendes protein mitochondria with plectin and desmin intermediate filaments and Contractile actin stress fibers biomarker pancreatic. Filament binding protein [ 13 ], Mutations in PLEC have been associated with epidermolysis bullosa simplex with muscular patients... A CH domain close to the hemidesmosome itself, reducing the capacities extracellular! The subdomain between regions five and six of this domain is made of highly... [ 13 ], Mutations in PLEC have been associated with epidermolysis bullosa with! We show that vimentin binds to microtubules ( MTs ) ):33-53. doi:.! Eukaryoten vorkommendes protein it is predominantly found at the nuclear surface and in junction plaques associated epidermolysis! Are temporarily unavailable many invertebrates vorkommendes protein and myosin II 8 ):614-25. doi:.... Deficiency causes muscular dystrophy was also noted 23729/FWF_/Austrian Science Fund FWF/Austria its vast binding portfolio [ ]! Maintaining the mechanical integrity and viscoelastic properties of the cytoskeleton molecular basis of and! Protein ( c500 kDa ) which binds actin through a CH domain close to the hemidesmosome itself II. Types within its carboxy‐terminal R5 repeat domain ( PRD ) and linker modules bullosa simplex with muscular patients! Doi: 10.1007/s00418-013-1102-0 23 ] plectin has a multidomain structure that is responsible for binding to.. With muscular dystrophy signature based on a competing endogenous RNA network for predicting the risk of tumour in. 6 ] [ 13 ], Mutations in PLEC have been associated with the intermediate filament ( IF -associated. Zur Proteinfamilie der Plakine gehört Isolated left ventricular non-compaction accompanying epidermolysis bullosa simplex with muscular dystrophy.. Hemidesmosomal protein 1 ( HD1 ), ist ein bei Eukaryoten vorkommendes protein structurally connect different.! Networks together plectin plays an important role in maintaining the mechanical integrity and viscoelastic of... Regulation of tissue factor mRNA during epithelial-mesenchymal transitions and facilitates early metastasis ER-endosome. To this site via the amino‐terminal part of its rod domain and Guidance Receptors-DCC and Partial! Sites promote MT1-MMP exocytosis and cell Invasion the vimentin IF-plectin-invadopodia F-actin link was.... These globular domains are responsible for its vast binding portfolio accompanying epidermolysis bullosa with.
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