Molecular mechanism of intermediate filament recognition by plakin proteins

Fiyaz Mohammed, Catharine Trieber, Michael Overduin, Martyn Chidgey

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1 Citation (Scopus)
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Abstract

The plakin family of cytolinkers interacts with intermediate filaments (IFs) through plakin repeat domain (PRD) and linker modules. Recent structure/function studies have established the molecular basis of envoplakin-PRD and periplakin-linker interactions with vimentin. Both plakin modules share a broad basic groove which recognizes acidic rod elements on IFs, a mechanism that is applicable to other plakin family members. This review postulates a universal IF engagement mechanism that illuminates the specific effects of pathogenic mutations associated with diseases including arrhythmogenic right ventricular cardiomyopathy, and reveals how diverse plakin proteins offer tailored IF tethering to ensure stable, dynamic and regulated cellular structures.
Original languageEnglish
Article number118801
JournalBiochimica et Biophysica Acta. Molecular Cell Research
Volume1867
Issue number11
Early online date23 Jul 2020
DOIs
Publication statusPublished - 1 Nov 2020

Keywords

  • Plakin
  • Plakin repeat domain
  • Linker module
  • Desmoplakin
  • Arrhythmogenic right ventricular cardiomyopathy
  • Intermediate filament

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