TY - JOUR
T1 - Ugene, a newly identified protein that is commonly overexpressed in cancer and binds uracil DNA gycosylase
AU - Guo, Chunguang
AU - Zhang, Xiaodong
AU - Fink, Stephen P.
AU - Platzer, Petra
AU - Wilson, Keith
AU - Willson, James K V
AU - Wang, Zhenghe
AU - Markowitz, Sanford D.
PY - 2008/8/1
Y1 - 2008/8/1
N2 - Expression microarrays identified a novel transcript, designated as Ugene, whose expression is absent in normal colon and colon adenomas, but that is commonly induced in malignant colon cancers. These findings were validated by real-time PCR and Northern blot analysis in an independent panel of colon cancer cases. In addition, Ugene expression was found to be elevated in many other common cancer types, including breast, lung, uterus, and ovary. Immunofluorescence of V5-tagged Ugene revealed it to have a nuclear localization. In a pull-down assay, uracil DNA glycosylase 2 (UNG2), an important enzyme in the base excision repair (BER) pathway, was identified as a partner protein that binds to Ugene. Coimmunoprecipitation and Western blot analysis confirmed the binding between the endogenous Ugene and UNG2 proteins. Using deletion constructs, we find that Ugene binds to the first 25 amino acids of the UNG2 NH2 terminus. We suggest that Ugene induction in cancer may contribute to the cancer phenotype by interacting with the BER pathway.
AB - Expression microarrays identified a novel transcript, designated as Ugene, whose expression is absent in normal colon and colon adenomas, but that is commonly induced in malignant colon cancers. These findings were validated by real-time PCR and Northern blot analysis in an independent panel of colon cancer cases. In addition, Ugene expression was found to be elevated in many other common cancer types, including breast, lung, uterus, and ovary. Immunofluorescence of V5-tagged Ugene revealed it to have a nuclear localization. In a pull-down assay, uracil DNA glycosylase 2 (UNG2), an important enzyme in the base excision repair (BER) pathway, was identified as a partner protein that binds to Ugene. Coimmunoprecipitation and Western blot analysis confirmed the binding between the endogenous Ugene and UNG2 proteins. Using deletion constructs, we find that Ugene binds to the first 25 amino acids of the UNG2 NH2 terminus. We suggest that Ugene induction in cancer may contribute to the cancer phenotype by interacting with the BER pathway.
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U2 - 10.1158/0008-5472.CAN-08-1259
DO - 10.1158/0008-5472.CAN-08-1259
M3 - Article
C2 - 18676834
AN - SCOPUS:51049100628
SN - 0008-5472
VL - 68
SP - 6118
EP - 6126
JO - Cancer research
JF - Cancer research
IS - 15
ER -