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Structural basis for heteromeric assembly and perinuclear organization of keratin filaments
- Structural basis for heteromeric assembly and perinuclear organization of keratin filaments
- Lee, Chang Hun; Kim, Min Sung; Chung, Byung Min; Leahy, Daniel J.; Coulombe, Pierre A.
- DGIST Authors
- Lee, Chang Hun
- Issue Date
- Nature Structural and Molecular Biology, 19(7), 707-715
- Article Type
- Amino Acid Sequence; Amino Acid Substitution; Animal Cell; Animal Experiment; Animal Tissue; Animals; Cell Culture; Cell Structure; Complex Formation; Controlled Study; Crystal Structure; Crystallography, X-Ray; Cytokeratin 14; Cytokeratin 5; Cytoplasm; Dimerization; Disulfide Bond; Disulfides; Epidermis; Epidermolysis Bullosa; Epidermolysis Bullosa Simplex; Humans; Hydrogen Bond; Hydrophobicity; Intermediate Filament; Keratinocyte; Keratinocytes; Keratins; Models, Molecular; Molecular Sequence Data; Mouse; Non-Human; Nucleotide Sequence; Polymerization; Priority Journal; Protein Domain; Protein Localization; Protein Structure; Sequence Homology, Amino Acid; Static Electricity
- There is as yet no high-resolution data regarding the structure and organization of keratin intermediate filaments, which are obligate heteropolymers providing vital mechanical support in epithelia. We report the crystal structure of interacting 2B regions from the central coiled-coil domains of keratins 5 and 14 (K5 and K14), expressed in progenitor keratinocytes of epidermis. The interface of the K5-K14 coiled-coil heterodimer has asymmetric salt bridges, hydrogen bonds and hydrophobic contacts, and its surface exhibits a notable charge polarization. A trans-dimer homotypic disulfide bond involving Cys367 in K14's stutter region occurs in the crystal and in skin keratinocytes, where it is concentrated in a keratin filament cage enveloping the nucleus. We show that K14-Cys367 impacts nuclear shape in cultured keratinocytes and that mouse epidermal keratinocytes lacking K14 show aberrations in nuclear structure, highlighting a new function for keratin filaments. © 2012 Nature America, Inc. All rights reserved.
- Nature Publishing Group
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