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Published 26 November 2001. doi:10.1083/jcb.200104063
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© The Rockefeller University Press, 0021-9525/2001/11/747 $5.00
The Journal of Cell Biology, Volume 155, Number 5, November 26, 2001 747-754

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 The nonhelical tail domain of keratin 14 promotes filament bundling and enhances the mechanical properties of keratin intermediate filaments in vitro

Olivier Bousquet1, Linglei Ma1, Soichiro Yamada2, Changhong Gu1, Toshihiro Idei3, Kenzo Takahashi4, Denis Wirtz2 and Pierre A. Coulombe1

1 Department of Biological Chemistry, School of Medicine
2 Department of Chemical Engineering, Johns Hopkins University, Baltimore, MD
3 Department of Dermatology, Kyoto University Graduate School of Medicine, Kyoto, Japan
4 Department of Dermatology, Gunma University School of Medicine, Maebashi, Japan

Address correspondence to Pierre A. Coulombe, Dept. of Biological Chemistry, Johns Hopkins University School of Medicine, 725 N. Wolfe St., Baltimore, MD 21205. Tel.: (410) 614-0510. Fax: (410) 614-0510. E-mail: coulombe{at}jhmi.edu

Keratin filaments arise from the copolymerization of type I and II sequences, and form a pancytoplasmic network that provides vital mechanical support to epithelial cells. Keratins 5 and 14 are expressed as a pair in basal cells of stratified epithelia, where they occur as bundled arrays of filaments. In vitro, bundles of K5–K14 filaments can be induced in the absence of cross-linkers, and exhibit enhanced resistance to mechanical strain. This property is not exhibited by copolymers of K5 and tailless K14, in which the nonhelical tail domain has been removed, or copolymers of K5 and K19, a type I keratin featuring a short tail domain. The purified K14 tail domain binds keratin filaments in vitro with specificity (kD ~2 µM). When transiently expressed in cultured cells, the K14 tail domain associates with endogenous keratin filaments. Utilization of the K14 tail domain as a bait in a yeast two-hybrid screen pulls out type I keratin sequences from a skin cDNA library. These data suggest that the tail domain of K14 contributes to the ability of K5–K14 filaments to self-organize into large bundles showing enhanced mechanical resilience in vitro.

Key Words: keratin; intermediate filament; tail domain; rheology; cross-linker


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