Molecular cloning and characterization of TPP36 and its isoform TPP32, novel substrates of Abl tyrosine kinase

FEBS Letters

Kawano, Youhei⁵  Okada, Masato¹  Maki, Kazushige⁵  Watanabe, Mamoru³  Toyama-Sorimachi, Noriko⁵  Miyasaka, Nobuyuki⁴  Nagata, Kisaburo²  Takao, Toshifumi⁶  Tsuchiya, Kiichiro³  Shinohara, Hisaaki⁵  Karasuyama, Hajime⁵  Kojima, Toshiyuki⁵ 

[1] Department of Oncology Research, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871, Japan;Department of Immunology, The Tokyo Metropolitan Institute of Medical Science, Tokyo 113-8613, Japan;Department of Gastroenterology and Hepatology, Tokyo Medical and Dental University Graduate School, Tokyo 113-8519, Japan;Department of Bioregulatory Medicine and Rheumatology, Tokyo Medical and Dental University Graduate School, Tokyo 113-8519, Japan;Department of Immune Regulation, Tokyo Medical and Dental University Graduate School, Tokyo 113-8519, Japan;Laboratory of Protein Profiling and Functional Proteomics, Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan

关键词: Abl;    Conformational change;    Isoform;    Nuclear localization signal;    Tyrosine phosphorylation;    BCR;    B cell receptor;    PTK;    protein tyrosine kinase;    FCS;    fetal calf serum;    EST;    expressed sequence tag;    CDV;    carnitine deficiency-associated gene expressed in ventricle;    SDS–PAGE;    sodium dodecyl sulfate–polyacrylamide gel electrophoresis;    Btk;    Bruton's tyrosine kinase;    EGF;    epidermal growth factor;    PDGF;    platelet-derived growth factor;   

DOI  :  10.1016/S0014-5793(03)00127-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have molecularly cloned TPP36, a novel 36 kDa protein with 281 amino acids that was identified as a protein phosphorylated in B progenitor cells following stimulation with pervanadate/H₂O₂. Analysis with anti-TPP36 antiserum revealed that TPP36 was expressed ubiquitously and had an isoform with 236 amino acids, designated TPP32. TPP36/32 were localized mainly in cytoplasm despite the presence of a typical nuclear localization signal sequence. These proteins were phosphorylated preferentially by Abl among a panel of tyrosine kinases examined. Phosphorylation of tyrosine 120 in TPP36/32 led to an apparent mobility shift in sodium dodecyl sulfate–polyacrylamide gel electrophoresis, suggesting conformational change in the phosphorylated protein. Thus, TPP36/32 appear to be novel substrates of Abl tyrosine kinase.

【 授权许可】

Unknown