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A novel ninein‐interaction protein, CGI‐99, blocks ninein phosphorylation by GSK3β and is highly expressed in brain tumors
Author(s) -
Howng Shen-Long,
Hsu Hui-Chun,
Cheng Tai-Shan,
Lee Yun-Lin,
Chang Li-Kwan,
Lu Pei-Jung,
Hong Yi-Ren
Publication year - 2004
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.2004.04.024
Subject(s) - phosphorylation , chemistry , microbiology and biotechnology , computational biology , biology , biochemistry
To explore more hNinein interacting proteins, the yeast two‐hybrid screening using ninein C‐terminal domain as bait protein was performed. One novel gene, CGI‐99 , was demonstrated to associate with hNinein in the yeast two‐hybrid method and in vitro GST pull‐down assay. Molecular characterization also showed that CGI‐99 possessed a transcriptional activity at the N‐terminal. In addition, CGI‐99 formed a dimer with the C‐terminal, which overlapped with hNinein binding site. In kinase assay, CGI‐99 binds to hNinein and completely blocks the phosphorylation of hNinein by GSK3β. Moreover, CGI‐99 was highly expressed in all brain tumors which is in agreement with the Northern blot analysis. Taken together, we have isolated a novel protein CGI‐99, which may be involved in the functional regulation of human ninein in the centrosome structure and may also be important in brain development and tumorigenesis.