دورية أكاديمية
أعرض في EDS

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

التفاصيل البيبلوغرافية
العنوان: Binding of the periplakin linker requires vimentin acidic residues D176 and E187.
المؤلفون: Odintsova E; Institute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, B15 2TT, UK., Mohammed F; Institute of Immunology and Immunotherapy, University of Birmingham, Birmingham, B15 2TT, UK., Trieber C; Department of Biochemistry, Faculty of Medicine & Dentistry, 474 Medical Sciences Building, University of Alberta, Edmonton, Alberta, T6G 2H7, Canada., Rodriguez-Zamora P; Institute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, B15 2TT, UK.; Instituto de Fisica, Universidad Nacional Autonoma de Mexico, Mexico City, 04510, Mexico., Al-Jassar C; Institute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, B15 2TT, UK., Huang TH; School of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK., Fogl C; Institute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, B15 2TT, UK.; The Binding Site, Birmingham, B15 1QT, UK., Knowles T; School of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK., Sridhar P; School of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK., Kumar J; Department of Biochemistry, Faculty of Medicine & Dentistry, 474 Medical Sciences Building, University of Alberta, Edmonton, Alberta, T6G 2H7, Canada., Jeeves M; Institute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, B15 2TT, UK., Chidgey M; Institute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, B15 2TT, UK. M.A.Chidgey@bham.ac.uk.; Institute of Clinical Sciences, University of Birmingham, Birmingham, B15 2TT, UK. M.A.Chidgey@bham.ac.uk., Overduin M; Department of Biochemistry, Faculty of Medicine & Dentistry, 474 Medical Sciences Building, University of Alberta, Edmonton, Alberta, T6G 2H7, Canada.
المصدر: Communications biology [Commun Biol] 2020 Feb 21; Vol. 3 (1), pp. 83. Date of Electronic Publication: 2020 Feb 21.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Nature Publishing Group UK Country of Publication: England NLM ID: 101719179 Publication Model: Electronic Cited Medium: Internet ISSN: 2399-3642 (Electronic) Linking ISSN: 23993642 NLM ISO Abbreviation: Commun Biol Subsets: MEDLINE
أسماء مطبوعة: Original Publication: London, United Kingdom : Nature Publishing Group UK, [2018]-
مواضيع طبية MeSH: Plakins/*chemistry , Plakins/*metabolism , Vimentin/*chemistry , Vimentin/*metabolism, Amino Acid Sequence ; Amino Acids, Acidic/chemistry ; Amino Acids, Acidic/genetics ; Amino Acids, Acidic/metabolism ; Aspartic Acid/metabolism ; Glutamic Acid/metabolism ; HeLa Cells ; Humans ; Intermediate Filaments/chemistry ; Intermediate Filaments/metabolism ; Models, Molecular ; Mutation, Missense ; Plakins/genetics ; Protein Binding/genetics ; Protein Interaction Domains and Motifs/genetics ; Protein Structure, Quaternary ; Vimentin/genetics
مستخلص: 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.
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معلومات مُعتمدة: United Kingdom WT_ Wellcome Trust; 094303/Z/10/Z United Kingdom WT_ Wellcome Trust; 099266/Z/12/Z United Kingdom WT_ Wellcome Trust; BB/P009840/1 United Kingdom BB_ Biotechnology and Biological Sciences Research Council
المشرفين على المادة: 0 (Amino Acids, Acidic)
0 (PPL protein, human)
0 (Plakins)
0 (Vimentin)
30KYC7MIAI (Aspartic Acid)
3KX376GY7L (Glutamic Acid)
تواريخ الأحداث: Date Created: 20200222 Date Completed: 20210617 Latest Revision: 20240328
رمز التحديث: 20240329
مُعرف محوري في PubMed: PMC7035337
DOI: 10.1038/s42003-020-0810-y
PMID: 32081916
قاعدة البيانات: MEDLINE
الوصف
تدمد:2399-3642
DOI:10.1038/s42003-020-0810-y