Functional Interaction between Nuclear Matrix-Associated Hbxap and Nf- Kappa B
Resource
EXPERIMENTAL CELL RESEARCH v.298 n.1 pp.133-143
Journal
EXPERIMENTAL CELL RESEARCH
Journal Volume
v.298
Journal Issue
n.1
Pages
133-143
Date Issued
2004
Date
2004
Author(s)
HUANG, JING-YI
SHEN, BIN-JON
TSAI, WEN-HAI
LEE, SHENG-CHUNG
Abstract
Hepatitis B virus X-associated protein (HBXAP) is a plant homeodomain ( PHD) finger-containing protein implicated in transcription regulation. However, the underlying molecular mechanism remains to be defined. Here, we show that HBXAP represses NF-kappaB-mediated gene activation in a dose- dependent manner. Our results showed that HBXAP and NF- kappaB colocalize to the nuclear matrix with specific physical interaction between them. HBXAP may depend on its nuclear matrix localization for its repression of NF-kappaB- mediated gene repression. A specific nuclear matrix targeting sequence of HBXAP was identified. The sequence is included in a region encompassing amino acids 688-722 that could form a coiled-coil structure. The 18-amino acid stretch lies at the core of that structure. The present results showed that either the coiled-coil conformation or the PHD finger domain is crucial for the transcription repression activity of HBXAP on NF -kappaB-mediated gene activation. Taken together, our results suggest that HBXAP may function as a negative regulator for TNF-alpha-induced, NF- kappaB-mediated gene activation. (C) 2004 Elsevier Inc. All rights reserved.
Subjects
HBXAP
NF-kappa B
nuclear matrix
p50
p65
PHD
SDGs