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| Subject Categories: Membranes & Transport |
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| The EMBO Journal
(2004) 23, 3216–3226, doi:10.1038/sj.emboj.7600333 Published online 22 July 2004 |
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| Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane fusion |
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| Ken-ichi Nakajima1, Hidenori Hirose1, 3, Mei Taniguchi1, Hirofumi Kurashina1, Kohei Arasaki1, Masami Nagahama1, Katsuko Tani1, Akitsugu Yamamoto2 and Mitsuo Tagaya1 |
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1 School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo, Japan 2 Department of Cell Biology, Nagahama Institute of Bio-Science and Technology, Nagahama, Shiga, Japan To whom correspondence should be addressed Mitsuo Tagaya, School of Life Sciences, Tokyo University of Pharmacy and Life Science, Horinouchi, Hachoiji, Tokyo 192-0392, Japan. Tel.: +81 426 77 7496; Fax: +81 426 76 8866; E-mail: tagaya@ls.toyaku.ac.jp 3 Present address: Central Pharmaceutical Research Institute, Japan Tabaco Inc., Takatsuki, Osaka 569-1125, Japan Received 5 February 2004; Accepted 24 June 2004; Published online 22 July 2004. |
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| Abstract |
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BNIP1, a member of the BH3-only protein family, was first discovered as one of the proteins that are capable of interacting with the antiapoptotic adenovirus E1B 19-kDa protein. Here we disclose a totally unexpected finding that BNIP1 is a component of the complex comprising syntaxin 18, an endoplasmic reticulum (ER)-located soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor (SNARE). Functional analysis revealed that BNIP1 participates in the formation of the ER network structure, but not in membrane trafficking between the ER and Golgi. Notably, a highly conserved leucine residue in the BH3 domain of BNIP1 plays an important role not only in the induction of apoptosis but also in the binding of  -SNAP, an adaptor that serves as a link between the chaperone ATPase NSF and SNAREs. This predicts that -SNAP may suppress apoptosis by competing with antiapoptotic proteins for the BH3 domain of BNIP1. Indeed, overexpression of -SNAP markedly delayed staurosporine-induced apoptosis. Our results shed light on possible crosstalk between apparently independent cellular events, apoptosis and ER membrane fusion. |
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| Keywords: -SNAP, apoptosis, BH3 domain, endoplasmic reticulum, membrane fusion |
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