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NMR structure and regulated expression in APL cell of human SH3BGRL3
Author(s) -
Xu Chao,
Zheng Peizheng,
Shen Shuhong,
Xu Yingqi,
Wei Ling,
Gao Hengjun,
Wang Shengnian,
Zhu Chongri,
Tang Yajun,
Wu Jihui,
Zhang Qinghua,
Shi Yunyu
Publication year - 2005
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/j.febslet.2005.04.011
Subject(s) - retinoic acid , cell culture , acute promyelocytic leukemia , thioredoxin , monoclonal antibody , promyelocytic leukemia protein , chemistry , microbiology and biotechnology , immunofluorescence , cytoplasm , downregulation and upregulation , nuclear protein , biology , antibody , transcription factor , biochemistry , immunology , gene , genetics
SH3 domain binding glutamic acid‐rich protein like 3 (SH3BGRL3) is the new member of thioredoxin (TRX) super family, whose posttranslational modified form was identified as tumor necrosis factor α (TNF‐α) inhibitory protein, TIP‐B1. In this paper, we determined its solution structure by multi‐dimensional nuclear magnetic resonance spectroscopy. The overall structure of human SH3BGRL3 conformed to a TRX‐like fold. To understand its function in vivo, the upregulated expression in acute promyelocytic leukemia cell line NB4 at both mRNA and protein level was elucidated. Immunofluorescence and immunohistochemistry staining with monoclonal antibody against SH3BGRL3 demonstrated that it was a cytoplasmic protein in both NB4 cell and human tissues. These results, as a whole, indicate that SH3BGRL3 may function as a regulator in all‐ trans retinoic acid‐induced pathway.