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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. Copyright © 2020 The Authors. Published by Elsevier B.V. All rights reserved.


Fiyaz Mohammed, Catharine Trieber, Michael Overduin, Martyn Chidgey. Molecular mechanism of intermediate filament recognition by plakin proteins. Biochimica et biophysica acta. Molecular cell research. 2020 Nov;1867(11):118801

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PMID: 32712070

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