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J. Biol. Chem., Vol. 279, Issue 25, 26425-26432, June 18, 2004

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Identification and Characterization of a Novel BASH N Terminus-associated Protein, BNAS2^*

Yasuhiro Imamura¶, Takashi Katahira¶, and Daisuke Kitamura||

From the Research Institute for Biological Sciences, Tokyo University of Science, 2669 Yamazaki, Noda-city, Chiba 278-0022, Japan and the Department of Pharmacology, Matsumoto Dental University, 1780 Gohbara, Hiro-oka, Shiojiri-city, Nagano 399-0781, Japan

A B cell-specific adaptor protein, BASH (also known as BLNK or SLP-65), is crucial for B cell receptor (BCR) signaling. BASH binds to various signaling intermediates, such as Btk, PLC2, Vav, and Grb2, through its well defined motifs. Although functional significance of such interactions has been documented, BASH-mediated signal transduction mechanism is not fully understood. Using the yeast two-hybrid system, we have identified a novel protein that binds to a conserved N-terminal domain of BASH, which we named BNAS2 (BASH N terminus associated protein 2). From its deduced amino acid sequence, BNAS2 is presumed to contain four transmembrane domains, which are included in a central MARVEL domain, and to localize to endoplasmic reticulum. BNAS2 was co-precipitated with BASH as well as Btk and ERK2 from a lysate of mouse B cell line. In the transfected cells, the exogenous BNAS2 was localized in a mesh-like structure in the cytoplasm resembling that of endoplasmic reticulum (ER) and nuclear membrane. BASH was co-localized with BNAS2 in a manner dependent on its N-terminal domain. RT-PCR analysis indicated that BNAS2 mRNA is expressed ubiquitously except for plasma cells. In chicken B cell line DT40, overexpression of BNAS2 resulted in an enhancement of BCR ligation-mediated transcriptional activation of Elk1, but not of NF-B, in a manner dependent on the dose of BNAS2. Thus BNAS2 may serve as a scaffold for signaling proteins such as BASH, Btk, and ERK at the ER and nuclear membrane and may facilitate ERK activation by signaling from cell-surface receptors.

Received for publication, April 2, 2004

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AB106870.

^* This work was supported by grants from the Ministry of Education, Culture, Sports, Science, and Technology (MEXT) in Japan and the Japan Society for the Promotion of Science. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ These authors contributed equally to this work.

^|| To whom correspondence should be addressed: Research Institute for Biological Sciences, Tokyo University of Science, 2669 Yamazaki, Noda-city, Chiba 278-0022, Japan. Tel.: 81-4-7121-4071; Fax: 81-4-7121-4079; E-mail: kitamura{at}rs.noda.tus.ac.jp.

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