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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45548

Title: Intermolecular binding between TIFA-FHA and TIFA-pT mediates tumor necrosis factor alpha stimulation and NF-κB activation.
Authors: Chia-Chi Flora Huang;Jui-Hung Weng;Tong-You Wade Wei;Pei-Yu Gabriel Wu;Pang-Hung Hsu;Yu-Hou Chen;Shun-Chang Wang;Dongyan Qin;Chin-Chun Hung;Shui-Tsung Chen;Andrew H.-J. Wang;John Y.-J. Shyy;Ming-Daw Tsai
Contributors: 國立臺灣海洋大學:生命科學系
Date: 2012
Issue Date: 2018-03-26T06:03:41Z
Publisher: Molecular Cell Biology
Abstract: Abstract: The forkhead-associated (FHA) domain recognizes phosphothreonine (pT) with high specificity and functional diversity. TIFA (TRAF-interacting protein with an FHA domain) is the smallest FHA-containing human protein. Its overexpression was previously suggested to provoke NF-κB activation, yet its exact roles in this signaling pathway and the underlying molecular mechanism remain unclear. Here we identify a novel threonine phosphorylation site on TIFA and show that this phosphorylated threonine (pT) binds with the FHA domain of TIFA, leading to TIFA oligomerization and TIFA-mediated NF-κB activation. Detailed analysis indicated that unphosphorylated TIFA exists as an intrinsic dimer and that the FHA-pT9 binding occurs between different dimers of TIFA. In addition, silencing of endogenous TIFA resulted in attenuation of tumor necrosis factor alpha (TNF-α)-mediated downstream signaling. We therefore propose that the TIFA FHA-pT9 binding provides a previously unidentified link between TNF-α stimulation and NF-κB activation. The intermolecular FHA-pT9 binding between dimers also represents a new mechanism for the FHA domain.
Relation: 32(14)
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45548
Appears in Collections:[生命科學系] 期刊論文

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