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XIAP‐associated factor 1 interacts with and attenuates the trans‐activity of four and a Half LIM protein 2
Author(s) -
Zhang Wenjing,
Yang Yi,
Jiang Bo,
Peng Junzhong,
Tu Shuiping,
Sardet Claude,
Zhang Yusheng,
Pang Roberta,
Hung Ivan F,
Tan V. P. Y.,
Lam Colin SC,
Wang Jide,
Wong Benjamin C.Y.
Publication year - 2011
Publication title -
molecular carcinogenesis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.254
H-Index - 97
eISSN - 1098-2744
pISSN - 0899-1987
DOI - 10.1002/mc.20705
Subject(s) - lim domain , biology , zinc finger , signal transducing adaptor protein , ubiquitin ligase , microbiology and biotechnology , two hybrid screening , ring finger domain , xiap , cytoplasm , repressor , suppressor , ring finger , cancer research , transcription factor , cancer , ubiquitin , genetics , gene , signal transduction , apoptosis , programmed cell death , caspase
Abstract XIAP‐associated factor 1(XAF1) is a tumor suppressor with its functional mechanisms not fully understood. The zinc‐finger cluster located at the N‐terminus is the only domain structure. Four and a half LIM domain protein 2 (FHL2) also contains a tandem zinc finger structure, and its protein functions as an important adaptor and modifier in protein–protein interactions. Both of their structures are relatively simple, while the association between them is still unclear. In this study, we detected the interaction between XAF1 and FHL2 by using the yeast two‐hybrid system. We identified FHL2 as a XAF1 binding protein. Furthermore, both XAF1 and FHL2 localized to the cytoplasm, mitochondria, and nucleus of gastric cancer cells. Over‐expression of XAF1 excluded FHL2 from the nucleus and suppressed the trans‐activity of FHL2 in stimulating the transcriptional activities of β‐catenin and AP‐1. In conclusion, our findings unraveled an antagonistic mechanism between a tumor suppressor and an oncoprotein in cancer cells. Mol. Carcinog. © 2010 Wiley‐Liss, Inc.