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Journal of Biochemistry Advance Access originally published online on November 20, 2008
Journal of Biochemistry 2009 145(2):185-191; doi:10.1093/jb/mvn155
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© The Authors 2008. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved

Nuclear Localization Mechanism of Hsp105β and its Possible Function in Mammalian Cells

Youhei Saito, Nobuyuki Yamagishi and Takumi Hatayama*

Department of Biochemistry and Molecular Biology, Kyoto Pharmaceutical University, Kyoto 607-8414, Japan

*To whom correspondence should be addressed. Tel: +81-75-595-4753, Fax: +81-75-595-4758, E-mail: hatayama{at}mb.kyoto-phu.ac.jp

Received September 30, 2008; Accepted November 9, 2008


  Abstract

Hsp105{alpha} and Hsp105β are mammalian stress proteins of the Hsp105/110 family. We have shown that Hsp105β localizes to the nucleus, whereas Hsp105{alpha} localizes to the cytoplasm of mammalian cells. Hsp105{alpha} localizes in the cytoplasm, as the nuclear export signal (NES) activity rather than nuclear localization signal (NLS) activity dominates in Hsp105{alpha}, due to suppression of the NLS activity. In this study, we determined the mechanisms behind the nuclear localization of Hsp105β, and revealed that the NES was suppressed by the N-terminal (amino acids 3–10) or C-terminal (amino acids 699–756) region of Hsp105β, and the NLS activity rather than NES activity seemed to dominate in Hsp105β. Furthermore, as Hsp105β which localizes in the nucleus, functioned as an inducer of Hsp70 in mammalian cells, Hsp105 family proteins may play an important role in the protection of cells against deleterious stressor together with Hsp70.

Key Words: Hsp105 Hsc70, Hsp70, nuclear export signal, nuclear localization signal

Abbreviations: Hsp, heat shock protein; Hsc70, heat shock cognate 70; NLS, nuclear localization signal; NES, nuclear export signal; LMB, leptomycin B; CRM1, chromosome maintenance region 1; SO, spliced out


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