Mechanism of intermediate filament recognition by plakin repeat domains revealed by envoplakin targeting of vimentin

Claudia Fogl, Fiyaz Mohammed, Caezar Al-Jassar, Mark Jeeves, Timothy J. Knowles, Penelope Rodriguez-Zamora, Scott A. White, Elena Odintsova, Michael Overduin () and Martyn Chidgey ()
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Claudia Fogl: School of Cancer Sciences, University of Birmingham
Fiyaz Mohammed: Institute of Immunology and Immunotherapy, University of Birmingham
Caezar Al-Jassar: School of Cancer Sciences, University of Birmingham
Mark Jeeves: School of Cancer Sciences, University of Birmingham
Timothy J. Knowles: School of Cancer Sciences, University of Birmingham
Penelope Rodriguez-Zamora: Nanoscale Physics Research Laboratory, School of Physics and Astronomy, University of Birmingham
Scott A. White: School of Biosciences, University of Birmingham
Elena Odintsova: Institute of Cancer and Genomic Sciences, University of Birmingham
Michael Overduin: School of Cancer Sciences, University of Birmingham
Martyn Chidgey: School of Cancer Sciences, University of Birmingham

Nature Communications, 2016, vol. 7, issue 1, 1-11

Abstract: Abstract Plakin proteins form critical connections between cell junctions and the cytoskeleton; their disruption within epithelial and cardiac muscle cells cause skin-blistering diseases and cardiomyopathies. Envoplakin has a single plakin repeat domain (PRD) which recognizes intermediate filaments through an unresolved mechanism. Herein we report the crystal structure of envoplakin’s complete PRD fold, revealing binding determinants within its electropositive binding groove. Four of its five internal repeats recognize negatively charged patches within vimentin via five basic determinants that are identified by nuclear magnetic resonance spectroscopy. Mutations of the Lys1901 or Arg1914 binding determinants delocalize heterodimeric envoplakin from intracellular vimentin and keratin filaments in cultured cells. Recognition of vimentin is abolished when its residues Asp112 or Asp119 are mutated. The latter slot intermediate filament rods into basic PRD domain grooves through electrosteric complementarity in a widely applicable mechanism. Together this reveals how plakin family members form dynamic linkages with cytoskeletal frameworks.

Date: 2016
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DOI: 10.1038/ncomms10827

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