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J. Biol. Chem., Vol. 275, Issue 44, 34521-34527, November 3, 2000
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From the To elucidate the function of keratins 8 and 18 (K8/18), major components of the intermediate filaments of simple
epithelia, we searched for K8/18-binding proteins by screening a yeast
two-hybrid library. We report here that human Mrj, a DnaJ/Hsp40 family
protein, directly binds to K18. Among the interactions between
DnaJ/Hsp40 family proteins and various intermediate filament proteins
that we tested using two-hybrid methods, Mrj specifically interacted with K18. Immunostaining with anti-Mrj antibody showed that Mrj colocalized with K8/18 filaments in HeLa cells. Mrj was
immunoprecipitated not only with K18, but also with the stress-induced
and constitutively expressed heat shock protein Hsp/c70. Mrj bound to
K18 through its C terminus and interacted with Hsp/c70 via its N
terminus, which contains the J domain. Microinjection of anti-Mrj
antibody resulted in the disorganization of K8/18 filaments, without
effects on the organization of actin filaments and microtubules. Taken together, these results suggest that Mrj may play an important role in
the regulation of K8/18 filament organization as a K18-specific co-chaperone working together with Hsp/c70.
Identification of Mrj, a DnaJ/Hsp40 Family Protein, as a
Keratin 8/18 Filament Regulatory Protein*
,,§,, and
Division of Biochemistry and the ¶ Cell
Stress Biology Research Group, Aichi Cancer Center Research Institute,
Chikusa-ku, Nagoya, Aichi 464-8681, Japan and the
§ Department of Neurosurgery, Mie University School of
Medicine, Edobashi, Tsu, Mie 514-8507, Japan
*
This work was supported in part by grants-in-aid for
scientific research and cancer research from the Ministry of Education, Science, Sports, and Culture of Japan; by the Japan Society for Promotion of Science Research for the Future; by a grant-in-aid for the
Second Term Comprehensive 10-Year Strategy for Cancer Control from the
Ministry of Health and Welfare, Japan; by a grant from
Bristol-Myers-Squibb; and by the Princess Takamatsu Cancer Research
Foundation.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Div. of
Biochemistry, Aichi Cancer Center Research Inst., 1-1 Kanokoden,
Chikusa-ku, Nagoya, Aichi 464-8681, Japan. Tel.: 81-52-762-6111 (ext.
7020); Fax: 81-52-763-5233; E-mail:
minagaki@aichi-cc.pref.aichi.jp.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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