Molecular mechanism of intermediate filament recognition by plakin proteins

Fiyaz Mohammed; Catharine Trieber; Michael Overduin; Martyn Chidgey

doi:10.1016/j.bbamcr.2020.118801

Molecular mechanism of intermediate filament recognition by plakin proteins

Fiyaz Mohammed, Catharine Trieber, Michael Overduin, Martyn Chidgey

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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 language	English
Article number	118801
Journal	Biochimica et Biophysica Acta. Molecular Cell Research
Volume	1867
Issue number	11
Early online date	23 Jul 2020
DOIs	https://doi.org/10.1016/j.bbamcr.2020.118801
Publication status	Published - 1 Nov 2020

Keywords

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

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10.1016/j.bbamcr.2020.118801Licence: Creative Commons: Attribution (CC BY)

Mohammed_et_al_2020_Molecular_mechanism_of_intermediate_filament_recognition_Biochimica_et_Biophysica_Acta_(BBA)-Molecular_Cell_ResearchFinal published version, 10.9 MBLicence: Creative Commons: Attribution (CC BY)

https://linkinghub.elsevier.com/retrieve/pii/S0167488920301592

The Molecular Basis of Gamma Delta T Cell Recognition in Health and Disease Enhancement funding - Linked to 17077
Willcox, B.
THE WELLCOME TRUST
1/02/17 → 31/05/21
Project: Research
The Molecular Basis of Gamma Delta T Cell Recognition in Health and Disease
Willcox, B.
THE WELLCOME TRUST
1/06/13 → 31/05/21
Project: Research
Structure and Function in Desmosomal Junctions
Overduin, M. & Chidgey, M.
THE WELLCOME TRUST
1/02/12 → 31/07/15
Project: Research

Cite this

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title = "Molecular mechanism of intermediate filament recognition by plakin proteins",

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.",

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AU - Chidgey, Martyn

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Molecular mechanism of intermediate filament recognition by plakin proteins

Abstract

Keywords

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Projects

The Molecular Basis of Gamma Delta T Cell Recognition in Health and Disease Enhancement funding - Linked to 17077

The Molecular Basis of Gamma Delta T Cell Recognition in Health and Disease

Structure and Function in Desmosomal Junctions

Cite this