FBI-1 enhances transcription of the nuclear factor-κB (NF-κB)-responsive E-selectin gene by nuclear localization of the p65 subunit of NF-κB

Dong Kee Lee, Jae Eun Kang, Hye Jin Park, Myung Hwa Kim, Tae Hee Yim, Jung Min Kim, Min Kyu Heo, Kyu Yeun Kim, Ho Jeong Kwon, Man Wook Hur

Research output: Contribution to journalArticle

48 Citations (Scopus)

Abstract

The POZ domain is a highly conserved protein-protein interaction motif found in many regulatory proteins. Nuclear factor-κB (NF-κB) plays a key role in the expression of a variety of genes in response to infection, inflammation, and stressful conditions. We found that the POZ domain of FBI-1 (factor that binds to the inducer of short transcripts of human immunodeficiency virus-1) interacted with the Rel homology domain of the p65 subunit of NF-κB in both in vivo and in vitro protein-protein interaction assays. FBI-1 enhanced NF-κB-mediated transcription of E-selectin genes in HeLa cells upon phorbol 12-myristate 13-acetate stimulation and overcame gene repression by IκBα or IκBβ. In contrast, the POZ domain of FBI-1, which is a dominant-negative form of FBI-1, repressed NF-κB-mediated transcription, and the repression was cooperative with IκBα or IκBβ. In contrast, the POZ domain tagged with a nuclear localization sequence polypeptide of FBI-1 enhanced NF-κB- responsive gene transcription, suggesting that the molecular interaction between the POZ domain and the Rel homology domain of p65 and the nuclear localization by the nuclear localization sequence are important in the transcription enhancement mediated by FBI-1. Confocal microscopy showed that FBI-1 increased NF-κB movement into the nucleus and increased the stability of NF-κB in the nucleus, which enhanced NF-κ-mediated transcription of the E-selectin gene. FBI-1 also interacted with IκBα and IκBβ.

Original languageEnglish
Pages (from-to)27783-27791
Number of pages9
JournalJournal of Biological Chemistry
Volume280
Issue number30
DOIs
Publication statusPublished - 2005 Jul 29

Fingerprint

E-Selectin
Transcription
Transcription Factors
Genes
Proteins
Protein Interaction Domains and Motifs
Molecular interactions
Confocal microscopy
Viruses
HeLa Cells
Confocal Microscopy
HIV-1
Assays
Acetates
BTB-POZ Domain
Inflammation
Peptides
Infection

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Lee, Dong Kee ; Kang, Jae Eun ; Park, Hye Jin ; Kim, Myung Hwa ; Yim, Tae Hee ; Kim, Jung Min ; Heo, Min Kyu ; Kim, Kyu Yeun ; Kwon, Ho Jeong ; Hur, Man Wook. / FBI-1 enhances transcription of the nuclear factor-κB (NF-κB)-responsive E-selectin gene by nuclear localization of the p65 subunit of NF-κB. In: Journal of Biological Chemistry. 2005 ; Vol. 280, No. 30. pp. 27783-27791.
@article{9b4b8be0449348aca45669998c15d276,
title = "FBI-1 enhances transcription of the nuclear factor-κB (NF-κB)-responsive E-selectin gene by nuclear localization of the p65 subunit of NF-κB",
abstract = "The POZ domain is a highly conserved protein-protein interaction motif found in many regulatory proteins. Nuclear factor-κB (NF-κB) plays a key role in the expression of a variety of genes in response to infection, inflammation, and stressful conditions. We found that the POZ domain of FBI-1 (factor that binds to the inducer of short transcripts of human immunodeficiency virus-1) interacted with the Rel homology domain of the p65 subunit of NF-κB in both in vivo and in vitro protein-protein interaction assays. FBI-1 enhanced NF-κB-mediated transcription of E-selectin genes in HeLa cells upon phorbol 12-myristate 13-acetate stimulation and overcame gene repression by IκBα or IκBβ. In contrast, the POZ domain of FBI-1, which is a dominant-negative form of FBI-1, repressed NF-κB-mediated transcription, and the repression was cooperative with IκBα or IκBβ. In contrast, the POZ domain tagged with a nuclear localization sequence polypeptide of FBI-1 enhanced NF-κB- responsive gene transcription, suggesting that the molecular interaction between the POZ domain and the Rel homology domain of p65 and the nuclear localization by the nuclear localization sequence are important in the transcription enhancement mediated by FBI-1. Confocal microscopy showed that FBI-1 increased NF-κB movement into the nucleus and increased the stability of NF-κB in the nucleus, which enhanced NF-κ-mediated transcription of the E-selectin gene. FBI-1 also interacted with IκBα and IκBβ.",
author = "Lee, {Dong Kee} and Kang, {Jae Eun} and Park, {Hye Jin} and Kim, {Myung Hwa} and Yim, {Tae Hee} and Kim, {Jung Min} and Heo, {Min Kyu} and Kim, {Kyu Yeun} and Kwon, {Ho Jeong} and Hur, {Man Wook}",
year = "2005",
month = "7",
day = "29",
doi = "10.1074/jbc.M504909200",
language = "English",
volume = "280",
pages = "27783--27791",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "30",

}

FBI-1 enhances transcription of the nuclear factor-κB (NF-κB)-responsive E-selectin gene by nuclear localization of the p65 subunit of NF-κB. / Lee, Dong Kee; Kang, Jae Eun; Park, Hye Jin; Kim, Myung Hwa; Yim, Tae Hee; Kim, Jung Min; Heo, Min Kyu; Kim, Kyu Yeun; Kwon, Ho Jeong; Hur, Man Wook.

In: Journal of Biological Chemistry, Vol. 280, No. 30, 29.07.2005, p. 27783-27791.

Research output: Contribution to journalArticle

TY - JOUR

T1 - FBI-1 enhances transcription of the nuclear factor-κB (NF-κB)-responsive E-selectin gene by nuclear localization of the p65 subunit of NF-κB

AU - Lee, Dong Kee

AU - Kang, Jae Eun

AU - Park, Hye Jin

AU - Kim, Myung Hwa

AU - Yim, Tae Hee

AU - Kim, Jung Min

AU - Heo, Min Kyu

AU - Kim, Kyu Yeun

AU - Kwon, Ho Jeong

AU - Hur, Man Wook

PY - 2005/7/29

Y1 - 2005/7/29

N2 - The POZ domain is a highly conserved protein-protein interaction motif found in many regulatory proteins. Nuclear factor-κB (NF-κB) plays a key role in the expression of a variety of genes in response to infection, inflammation, and stressful conditions. We found that the POZ domain of FBI-1 (factor that binds to the inducer of short transcripts of human immunodeficiency virus-1) interacted with the Rel homology domain of the p65 subunit of NF-κB in both in vivo and in vitro protein-protein interaction assays. FBI-1 enhanced NF-κB-mediated transcription of E-selectin genes in HeLa cells upon phorbol 12-myristate 13-acetate stimulation and overcame gene repression by IκBα or IκBβ. In contrast, the POZ domain of FBI-1, which is a dominant-negative form of FBI-1, repressed NF-κB-mediated transcription, and the repression was cooperative with IκBα or IκBβ. In contrast, the POZ domain tagged with a nuclear localization sequence polypeptide of FBI-1 enhanced NF-κB- responsive gene transcription, suggesting that the molecular interaction between the POZ domain and the Rel homology domain of p65 and the nuclear localization by the nuclear localization sequence are important in the transcription enhancement mediated by FBI-1. Confocal microscopy showed that FBI-1 increased NF-κB movement into the nucleus and increased the stability of NF-κB in the nucleus, which enhanced NF-κ-mediated transcription of the E-selectin gene. FBI-1 also interacted with IκBα and IκBβ.

AB - The POZ domain is a highly conserved protein-protein interaction motif found in many regulatory proteins. Nuclear factor-κB (NF-κB) plays a key role in the expression of a variety of genes in response to infection, inflammation, and stressful conditions. We found that the POZ domain of FBI-1 (factor that binds to the inducer of short transcripts of human immunodeficiency virus-1) interacted with the Rel homology domain of the p65 subunit of NF-κB in both in vivo and in vitro protein-protein interaction assays. FBI-1 enhanced NF-κB-mediated transcription of E-selectin genes in HeLa cells upon phorbol 12-myristate 13-acetate stimulation and overcame gene repression by IκBα or IκBβ. In contrast, the POZ domain of FBI-1, which is a dominant-negative form of FBI-1, repressed NF-κB-mediated transcription, and the repression was cooperative with IκBα or IκBβ. In contrast, the POZ domain tagged with a nuclear localization sequence polypeptide of FBI-1 enhanced NF-κB- responsive gene transcription, suggesting that the molecular interaction between the POZ domain and the Rel homology domain of p65 and the nuclear localization by the nuclear localization sequence are important in the transcription enhancement mediated by FBI-1. Confocal microscopy showed that FBI-1 increased NF-κB movement into the nucleus and increased the stability of NF-κB in the nucleus, which enhanced NF-κ-mediated transcription of the E-selectin gene. FBI-1 also interacted with IκBα and IκBβ.

UR - http://www.scopus.com/inward/record.url?scp=23044461830&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=23044461830&partnerID=8YFLogxK

U2 - 10.1074/jbc.M504909200

DO - 10.1074/jbc.M504909200

M3 - Article

C2 - 15917220

AN - SCOPUS:23044461830

VL - 280

SP - 27783

EP - 27791

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 30

ER -