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Molecular cloning and characterization of Byp, a murine receptor‐type tyrosine phosphatase similar to human DEP‐1
Author(s) -
Kuramochi Satomi,
Matsuda Satoru,
Matsuda Yoichi,
Saitoh Toshiyuki,
Ohsugi Miho,
Yamamoto Tadashi
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01415-2
Subject(s) - fyn , protein tyrosine phosphatase , microbiology and biotechnology , tyrosine phosphorylation , complementary dna , chemistry , sh2 domain , receptor tyrosine kinase , tyrosine , phosphorylation , tyrosine kinase , gene , biology , proto oncogene tyrosine protein kinase src , biochemistry , receptor
Novel murine cDNAs encoding a receptor‐like protein tyrosine phosphatase, termed Byp (HPTP b eta‐like tyrosine p hosphatase) 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.