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

  1. Get@NRC: MAP1B and clathrin are novel interacting partners of the giant cyto-linker dystonin (Opens in a new window)
DOIResolve DOI:
AuthorSearch for: ; Search for: ; Search for:
Journal titleJournal of Proteome Research
Pages51185127; # of pages: 10
Subjectbullous pemphigoid antigen 1; clathrin; cytoskeleton protein; microtubule associated protein 5; plakin; animal cell; animal tissue; article; degenerative disease; dystonia; immunofluorescence; immunoprecipitation; mouse; nonhuman; nucleotide sequence; priority journal; protein domain; protein interaction; protein phosphorylation; Animals; 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
AbstractDystonin 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.
Publication date
AffiliationNational Research Council Canada (NRC-CNRC); NRC Institute for Biological Sciences (IBS-ISB)
Peer reviewedYes
NPARC number21271370
Export citationExport as RIS
Report a correctionReport a correction
Record identifier18ffe76a-d1e4-4324-bf74-4438dec0a96a
Record created2014-03-24
Record modified2016-05-09
Bookmark and share
  • Share this page with Facebook (Opens in a new window)
  • Share this page with Twitter (Opens in a new window)
  • Share this page with Google+ (Opens in a new window)
  • Share this page with Delicious (Opens in a new window)