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Genes to Cells (2005) 10, 575-594. doi:10.1111/j.1365-2443.2005.00860.x
© 2005 Blackwell Publishing or its licensors
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Tisp40, a spermatid specific bZip transcription factor, functions by binding to the unfolded protein response element via the Rip pathway

Ippei Nagamori1, Norikazu Yabuta1, Takayuki Fujii1, Hiromitsu Tanaka2, Kentaro Yomogida2, Yoshitake Nishimune2 and Hiroshi Nojima1,*

1 Department of Molecular Genetics, and 2 Department of Science for Laboratory Animal Experimentation, Research Institute for Microbial Diseases, Osaka University, Yamadaoka 3-1, Suita City, Osaka, Japan

TISP40, a mouse spermatid-specific gene, encodes a CREB/CREM family transcription factor that is predominantly expressed during spermiogenesis. We report here that TISP40 generates two types of proteins, Tisp40{alpha} and Tisp40ß, both of which contain a transmembrane domain and localize to the endoplasmic reticulum (ER). In contrast, mutant proteins lacking the transmembrane domain (Tisp40{alpha}/ß{Delta}TM) primarily localize to the nucleus. Endoglycosidase H treatment shows that the C-terminus of Tisp40{alpha}/ß is glycosylated. Protease experiments demonstrate that Tisp40{alpha}/ß are Type II transmembrane proteins that are released into the nucleus by a two-step cleavage mechanism called ‘regulated intramembrane proteolysis’ (Rip). Unlike previously published observations, Tisp40{alpha} does not bind to the NF-{kappa}B site; instead, it specifically binds to the unfolded protein response element (UPRE). Luciferase assays reveal that Tisp40ß{Delta}TM activates transcription through UPRE. Northern blot analysis shows that Tisp40{alpha}/ß{Delta}TM proteins up-regulate EDEM (ER degradation of enhancing {alpha}-manosidase-like protein) mRNA. These observations unveil a novel event in mouse spermiogenesis and show that the final stage of trans-criptional regulation is controlled by the Rip pathway.

Communicated by: Hiroshi Hamada

* Correspondence: E-mail: snj-0212{at}biken.osaka-u.ac.jp




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