Molecular mechanism of intermediate filament recognition by plakin proteins.

Fiyaz Mohammed, Catharine Trieber, Michael Overduin, Martyn Chidgey

Journal: Biochimica et biophysica acta. Molecular cell research 2021;1867(11):118801

PMID: 32712070

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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.

Address: Institute of Immunology and Immunotherapy, University of Birmingham, Birmingham B15 2TT, UK. Electronic address: [email protected].; Department of Biochemistry, Faculty of Medicine and Dentistry, 474 Medical Sciences Building, University of Alberta, Edmonton, Alberta T6G 2H7, Canada. Electronic address: [email protected].; Department of Biochemistry, Faculty of Medicine and Dentistry, 474 Medical Sciences Building, University of Alberta, Edmonton, Alberta T6G 2H7, Canada. Electronic address: [email protected].; Institute of Clinical Sciences, University of Birmingham, Birmingham B15 2TT, UK. Electronic address: [email protected].

DOI: 10.1016/j.bbamcr.2020.118801

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MeSH Terms: Amino Acid Sequence, Arrhythmogenic Right Ventricular Dysplasia, Humans, Intermediate Filaments, Mutation, Plakins, Protein Binding, Protein Domains, Vimentin