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MAP1B and clathrin are novel interacting partners of the giant cyto-linker dystonin

Par Conseil national de recherches du Canada

DOITrouver le DOI : https://doi.org/10.1021/pr200564g
AuteurRechercher : ; Rechercher : 1; Rechercher :
Affiliation
  1. Conseil national de recherches du Canada. Institut des sciences biologiques du CNRC
FormatTexte, Article
Sujetbullous pemphigoid antigen 1; clathrin; cytoskeleton protein; microtubule associated protein 5; plakin; animal cell; animal tissue; degenerative disease; dystonia; immunofluorescence; immunoprecipitation; mouse; nucleotide sequence; protein domain; protein interaction; protein phosphorylation; Brain; Carrier Proteins; Cell Line; Cercopithecus aethiops; Clathrin Heavy Chains; COS Cells; Cytoskeletal Proteins; Fluorescent Antibody Technique, Indirect; Gene Expression; Mice; Microtubule-Associated Proteins; Nerve Tissue Proteins; Protein Binding; Protein Interaction Domains and Motifs; Protein Interaction Mapping; Rats; Triskelion
Résumé
Dystonin is a large multidomain cytoskeletal-associated protein that plays an essential role in the nervous system. Loss of dystonin results in neuromuscular dysfunction and early death in a mouse mutant called dystonia musculorum. Conserved among related proteins, the plakin domain is a defining feature of all major dystonin isoforms, yet its interactions have not been explored in detail. The purpose of the present study was to identify novel interacting partners of the plakin domain of the neuronal isoform of dystonin (dystonin-a). Newly identified interacting proteins discovered through a pull-down assay were validated using coimmunoprecipitation, coimmunofluorescence, and proximity ligation assays. Microtubule associated protein 1B (MAP1B), a microtubule stabilizing protein, and clathrin heavy chain, the major component of the clathrin triskelion, were identified as interaction partners for dystonin-a. Increased levels of phosphorylated MAP1B suggest a misregulation of MAP1B and a potentially novel component of the dt pathology. This work will further facilitate our understanding of how cytoskeletal proteins can affect and regulate neurodegenerative disorders. © 2011 American Chemical Society.
Date de publication
Dans
  • Journal of Proteome Research 10, nº 11 (2011) : 5118–5127.
Langueanglais
Publications évaluées par des pairsOui
Numéro NPARC21271370
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Identificateur de l’enregistrement18ffe76a-d1e4-4324-bf74-4438dec0a96a
Enregistrement créé2014-03-24
Enregistrement modifié2020-04-21
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