Molecular cloning and characterization of Byp, a murine receptor‐type tyrosine phosphatase similar to human DEP‐1

FEBS Letters

Kuramochi, Satomi²  Matsuda, Yoichi¹  Saitoh, Toshiyuki¹  Yamamoto, Tadashi²  Ohsugi, Miho²  Matsuda, Satoru¹ 

[1] Division of Genetics, National Institute of Radiological Sciences, 4-9-1, Anagawa, Inage-ku, Chiba 263, Japan;The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108, Japan

关键词: Protein tyrosine phosphatase;    Tyrosine phosphorylation;    Fyn tyrosine kinase;   

DOI  :  10.1016/0014-5793(95)01415-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Novel murine cDNAs encoding a receptor-like protein tyrosine phosphatase, termed Byp (HPTP beta-like tyrosine phosphatase) were cloned. The putative Byp protein consists of 1238 amino acids, which possesses a single catalytic domain in the cytoplasmic region. The extracellular region comprises eight repeats of a fibronectin type III module and contains multiple N-glycosylation sites. The byp mRNA was 7.7-kb long and expressed in every tissue examined, its level being high in the brain and kidney. Transfection of the byp cDNA expression plasmid into COS7 cells resulted in the expression of a 220-kDa tyrosine phosphorylated protein. Furthermore, co-expression of Byp and the Src family kinase Fyn increased the level of tyrosine phosphorylation of Byp, suggesting that Byp was tyrosine-phosphorylated by Fyn. Finally, the byp gene was located to mouse chromosome 2E1–2E2 and rat chromosome 3832–3833.

【 授权许可】

Unknown