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Structural basis for heteromeric assembly and perinuclear organization of keratin filaments

Title
Structural basis for heteromeric assembly and perinuclear organization of keratin filaments
Authors
Lee, Chang HunKim, Min SungChung, Byung MinLeahy, Daniel J.Coulombe, Pierre A.
DGIST Authors
Lee, Chang Hun
Issue Date
2012-07
Citation
Nature Structural and Molecular Biology, 19(7), 707-715
Type
Article
Article Type
Article
Keywords
Amino Acid SequenceAmino Acid SubstitutionAnimal CellAnimal ExperimentAnimal TissueAnimalsCell CultureCell StructureComplex FormationControlled StudyCrystal StructureCrystallography, X-RayCytokeratin 14Cytokeratin 5CytoplasmDimerizationDisulfide BondDisulfidesEpidermisEpidermolysis BullosaEpidermolysis Bullosa SimplexHumansHydrogen BondHydrophobicityIntermediate FilamentKeratinocyteKeratinocytesKeratinsModels, MolecularMolecular Sequence DataMouseNon-HumanNucleotide SequencePolymerizationPriority JournalProtein DomainProtein LocalizationProtein StructureSequence Homology, Amino AcidStatic Electricity
ISSN
1545-9993
Abstract
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.
URI
http://hdl.handle.net/20.500.11750/5373
DOI
10.1038/nsmb.2330
Publisher
Nature Publishing Group
Related Researcher
  • Author Lee, Chang-Hun  
  • Research Interests Structure-Function relationship of cytoskeletal proteins and membrane proteins; Structure-based design of biomolecules and drugs; Development of drug delivery system in skin
Files:
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Collection:
School of Undergraduate Studies1. Journal Articles


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