Keratin attenuates tumor necrosis factor-induced cytotoxicity through association with TRADD

doi:10.1083/jcb.200103078

Published 29 October 2001. doi:10.1083/jcb.200103078

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© The Rockefeller University Press, 0021-9525/2001/10/415 $5.00
The Journal of Cell Biology, Volume 155, Number 3, October 29, 2001 415-426

Article

Keratin attenuates tumor necrosis factor–induced cytotoxicity through association with TRADD

Hiroyasu Inada¹, Ichiro Izawa¹, Miwako Nishizawa¹, Eriko Fujita⁴, Tohru Kiyono², Toshitada Takahashi³, Takashi Momoi⁴ and Masaki Inagaki¹

¹ Division of Biochemistry, Aichi Cancer Center Research Institute, Aichi 464-8681, Japan
² Division of Virology, Aichi Cancer Center Research Institute, Aichi 464-8681, Japan
³ Division of Immunology, Aichi Cancer Center Research Institute, Aichi 464-8681, Japan
⁴ Division of Development and Differentiation, National Institute of Neuroscience, NCNP, Tokyo 187-8502, Japan

Address correspondence to Dr. Masaki Inagaki, Division of Biochemistry, Aichi Cancer Center Research Institute, 1-1 Kanokoden, Chikusaku, Nagoya, Aichi 464-8681, Japan. Tel.: 81-52-762-6111 (ext. 7020). Fax: 81-52-763-5233. E-mail: minagaki{at}aichi-cc.jp

Keratin 8 and 18 (K8/18) are the major components of intermediatefilament (IF) proteins of simple or single-layered epithelia.Recent data show that normal and malignant epithelial cellsdeficient in K8/18 are nearly 100 times more sensitive to tumornecrosis factor (TNF)–induced cell death. We have nowidentified human TNF receptor type 1 (TNFR1)–associateddeath domain protein (TRADD) to be the K18-interacting protein.Among IF proteins tested in two-hybrid systems, TRADD specificallybound K18 and K14, type I (acidic) keratins. The COOH-terminalregion of TRADD interacted with the coil Ia of the rod domainof K18. Endogenous TRADD coimmunoprecipitated with K18, andcolocalized with K8/18 filaments in human mammary epithelialcells. Overexpression of the NH₂ terminus (amino acids 1–270)of K18 containing the TRADD-binding domain as well as overexpressionof K8/18 in SW13 cells, which are devoid of keratins, renderedthe cells more resistant to killing by TNF. We also showed thatoverexpressed NH₂ termini of K18 and K8/18 were associated withendogenous TRADD in SW13 cells, resulting in the inhibitionof caspase-8 activation. These results indicate that K18 maysequester TRADD to attenuate interactions between TRADD andactivated TNFR1 and moderate TNF-induced apoptosis in simpleepithelial cells.

Key Words: apoptosis; keratin 8; keratin 18; TNF; TRADD

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