Structural highlights
Disease
K1C14_HUMAN Epidermolysis bullosa simplex, Dowling-Meara type;Localized epidermolysis bullosa simplex;Dermatopathia pigmentosa reticularis;Naegeli-Franceschetti-Jadassohn syndrome;Epidermolysis bullosa simplex with mottled pigmentation;Generalized epidermolysis bullosa simplex, non-Dowling-Meara type;KRT14-related epidermolysis bullosa simplex. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
Function
K1C14_HUMAN The nonhelical tail domain is involved in promoting KRT5-KRT14 filaments to self-organize into large bundles and enhances the mechanical properties involved in resilience of keratin intermediate filaments in vitro.[1]
Publication Abstract from PubMed
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.
Structural basis for heteromeric assembly and perinuclear organization of keratin filaments.,Lee CH, Kim MS, Chung BM, Leahy DJ, Coulombe PA Nat Struct Mol Biol. 2012 Jun 17;19(7):707-15. doi: 10.1038/nsmb.2330. PMID:22705788[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bousquet O, Ma L, Yamada S, Gu C, Idei T, Takahashi K, Wirtz D, Coulombe PA. The nonhelical tail domain of keratin 14 promotes filament bundling and enhances the mechanical properties of keratin intermediate filaments in vitro. J Cell Biol. 2001 Nov 26;155(5):747-54. Epub 2001 Nov 26. PMID:11724817 doi:http://dx.doi.org/10.1083/jcb.200104063
- ↑ Lee CH, Kim MS, Chung BM, Leahy DJ, Coulombe PA. Structural basis for heteromeric assembly and perinuclear organization of keratin filaments. Nat Struct Mol Biol. 2012 Jun 17;19(7):707-15. doi: 10.1038/nsmb.2330. PMID:22705788 doi:10.1038/nsmb.2330
