NMR structure and regulated expression in APL cell of human SH3BGRL3.
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 alpha (TNF-alpha) 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.
Xu
Chao
C
Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China.
Zheng
Peizheng
P
Shen
Shuhong
S
Xu
Yingqi
Y
Wei
Ling
L
Gao
Hengjun
H
Wang
Shengnian
S
Zhu
Chongri
C
Tang
Yajun
Y
Wu
Jihui
J
Zhang
Qinghua
Q
Shi
Yunyu
Y
D000595:Amino Acid Sequence; D001483:Base Sequence; D017931:DNA Primers; D018076:DNA, Complementary; D006801:Humans; D007150:Immunohistochemistry; D015473:Leukemia, Promyelocytic, Acute / Q000378:metabolism* / Q000473:pathology; D008969:Molecular Sequence Data; D009124:Muscle Proteins / Q000737:chemistry / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D020133:Reverse Transcriptase Polymerase Chain Reaction; D017386:Sequence Homology, Amino Acid
D017931:DNA Primers; D018076:DNA, Complementary; D009124:Muscle Proteins; C104671:SH3BGR protein, human