Binding of the periplakin linker requires vimentin acidic residues D176 and E187


Por: Odintsova, Elena, Mohammed, Fiyaz, Trieber, Catharine, Rodriguez-Zamora, Penelope, Al-Jassar, Caezar, Huang T.-H., Fogl, Claudia, Knowles, Timothy, Sridhar, Pooja, Kumar, Jitendra, Jeeves, Mark, Chidgey, Martyn, Overduin, Michael

Publicada: 1 ene 2020
Resumen:
Plakin proteins form connections that link the cell membrane to the intermediate filament cytoskeleton. Their interactions are mediated by a highly conserved linker domain through an unresolved mechanism. Here analysis of the human periplakin linker domain structure reveals a bi-lobed module transected by an electropositive groove. Key basic residues within the periplakin groove are vital for co-localization with vimentin in human cells and compromise direct binding which also requires acidic residues D176 and E187 in vimentin. We propose a model whereby basic periplakin linker domain residues recognize acidic vimentin side chains and form a complementary binding groove. The model is shared amongst diverse linker domains and can be used to investigate the effects of pathogenic mutations in the desmoplakin linker associated with arrhythmogenic right ventricular cardiomyopathy. Linker modules either act solely or collaborate with adjacent plakin repeat domains to create strong and adaptable tethering within epithelia and cardiac muscle.

Filiaciones:
Odintsova, Elena:
 Institute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, B15 2TT, United Kingdom

 Univ Birmingham, Inst Canc & Genom Sci, Birmingham B15 2TT, W Midlands, England

Mohammed, Fiyaz:
 Institute of Immunology and Immunotherapy, University of Birmingham, Birmingham, B15 2TT, United Kingdom

 Univ Birmingham, Inst Immunol & Immunotherapy, Birmingham B15 2TT, W Midlands, England

Trieber, Catharine:
 Department of Biochemistry, Faculty of Medicine & Dentistry, University of Alberta, 474 Medical Sciences Building, Edmonton, AB T6G 2H7, Canada

 Univ Alberta, Fac Med & Dent, Dept Biochem, 474 Med Sci Bldg, Edmonton, AB T6G 2H7, Canada

Rodriguez-Zamora, Penelope:
 Institute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, B15 2TT, United Kingdom

 Instituto de Fisica, Universidad Nacional Autonoma de MexicoMexico City 04510, Mexico

 Univ Birmingham, Inst Canc & Genom Sci, Birmingham B15 2TT, W Midlands, England

 Univ Nacl Autonoma Mexico, Inst Fis, Mexico City 04510, DF, Mexico

Al-Jassar, Caezar:
 Institute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, B15 2TT, United Kingdom

 Univ Birmingham, Inst Canc & Genom Sci, Birmingham B15 2TT, W Midlands, England

Huang T.-H.:
 School of Biosciences, University of Birmingham, Birmingham, B15 2TT, United Kingdom

Fogl, Claudia:
 Institute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, B15 2TT, United Kingdom

 Binding Site, Birmingham, B15 1QT, United Kingdom

 Univ Birmingham, Inst Canc & Genom Sci, Birmingham B15 2TT, W Midlands, England

 Binding Site, Birmingham B15 1QT, W Midlands, England

Knowles, Timothy:
 School of Biosciences, University of Birmingham, Birmingham, B15 2TT, United Kingdom

 Univ Birmingham, Sch Biosci, Birmingham B15 2TT, W Midlands, England

Sridhar, Pooja:
 School of Biosciences, University of Birmingham, Birmingham, B15 2TT, United Kingdom

 Univ Birmingham, Sch Biosci, Birmingham B15 2TT, W Midlands, England

Kumar, Jitendra:
 Department of Biochemistry, Faculty of Medicine & Dentistry, University of Alberta, 474 Medical Sciences Building, Edmonton, AB T6G 2H7, Canada

 Univ Alberta, Fac Med & Dent, Dept Biochem, 474 Med Sci Bldg, Edmonton, AB T6G 2H7, Canada

Jeeves, Mark:
 Institute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, B15 2TT, United Kingdom

 Univ Birmingham, Inst Canc & Genom Sci, Birmingham B15 2TT, W Midlands, England

Chidgey, Martyn:
 Institute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, B15 2TT, United Kingdom

 Institute of Clinical Sciences, University of Birmingham, Birmingham, B15 2TT, United Kingdom

 Univ Birmingham, Inst Canc & Genom Sci, Birmingham B15 2TT, W Midlands, England

 Univ Birmingham, Inst Clin Sci, Birmingham B15 2TT, W Midlands, England

Overduin, Michael:
 Department of Biochemistry, Faculty of Medicine & Dentistry, University of Alberta, 474 Medical Sciences Building, Edmonton, AB T6G 2H7, Canada

 Univ Alberta, Fac Med & Dent, Dept Biochem, 474 Med Sci Bldg, Edmonton, AB T6G 2H7, Canada
ISSN: 23993642
Editorial
NATURE PUBLISHING GROUP, 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA, Estados Unidos America
Tipo de documento: Article
Volumen: 3 Número: 1
Páginas: 83
WOS Id: 000517308600003
ID de PubMed: 32081916

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