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Transglutaminase 2 mediates polymer formation of I-kappaBalpha through C-terminal glutamine cluster.

Recently we reported that transglutaminase 2 (TGase 2) activates nuclear factor-kappaB (NF-kappaB) independently of I-kappaB kinase (IKK) activation, by inducing cross-linking and protein polymer formation of inhibitor of nuclear factor-kappaBalpha (I-kappaBalpha). TGase 2 catalyzes covalent isopept... Full description

Journal Title: The Journal of biological chemistry November 17, 2006, Vol.281(46), pp.34965-34972
Main Author: Park, Sung-Soo
Other Authors: Kim, Jung-Mo , Kim, Dae-Seok , Kim, In-Hoo , Kim, Soo-Youl
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0021-9258
Link: http://search.proquest.com/docview/68134110/?pq-origsite=primo
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title: Transglutaminase 2 mediates polymer formation of I-kappaBalpha through C-terminal glutamine cluster.
format: Article
creator:
  • Park, Sung-Soo
  • Kim, Jung-Mo
  • Kim, Dae-Seok
  • Kim, In-Hoo
  • Kim, Soo-Youl
subjects:
  • Amino Acid Sequence–Chemistry
  • Biopolymers–Metabolism
  • Gtp-Binding Proteins–Metabolism
  • Glutamine–Metabolism
  • Humans–Chemistry
  • I-Kappa B Proteins–Metabolism
  • Nf-Kappa B–Metabolism
  • Transglutaminases–Metabolism
  • Biopolymers
  • I-Kappa B Proteins
  • Nf-Kappa B
  • Glutamine
  • Transglutaminase 2
  • Transglutaminases
  • Gtp-Binding Proteins
ispartof: The Journal of biological chemistry, November 17, 2006, Vol.281(46), pp.34965-34972
description: Recently we reported that transglutaminase 2 (TGase 2) activates nuclear factor-kappaB (NF-kappaB) independently of I-kappaB kinase (IKK) activation, by inducing cross-linking and protein polymer formation of inhibitor of nuclear factor-kappaBalpha (I-kappaBalpha). TGase 2 catalyzes covalent isopeptide bond formation between the peptide bound-glutamine and the lysine residues. Using matrix-assisted laser desorption ionization time-of-flight mass spectra analysis of I-kappaBalpha polymers cross-linked by TGase 2, as well as synthetic peptides in an in vitro competition assay, we identified a glutamine cluster at the C terminus of I-kappaBalpha (amino acids 266-268) that appeared to play a key role in the formation of I-kappaBalpha polymers. Although there appeared to be no requirement for specific lysine residues, we found a considerably higher preference for the use of lysine residues at positions 21, 22, and 177 in TGase 2-mediated cross-linking of I-kappaBalpha. We demonstrated that synthetic peptides encompassing the glutamine cluster at amino acid positions 266-268 reversed I-kappaBalpha polymerization in vitro. Furthermore, the depletion of free I-kappaBalpha in EcR/TG cells was completely rescued in vivo by transfection of mutant I-kappaBalphas in glutamine sites (Q266G, Q267G, and Q313G) as well as in a lysine site (K177G). These findings provide additional clues into the mechanism by which TGase 2 contributes to the inflammatory process via activation of NF-kappaB.
language: eng
source:
identifier: ISSN: 0021-9258
fulltext: fulltext
issn:
  • 00219258
  • 0021-9258
url: Link


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titleTransglutaminase 2 mediates polymer formation of I-kappaBalpha through C-terminal glutamine cluster.
creatorPark, Sung-Soo ; Kim, Jung-Mo ; Kim, Dae-Seok ; Kim, In-Hoo ; Kim, Soo-Youl
contributorPark, Sung-Soo (correspondence author) ; Park, Sung-Soo (record owner)
ispartofThe Journal of biological chemistry, November 17, 2006, Vol.281(46), pp.34965-34972
identifierISSN: 0021-9258
subjectAmino Acid Sequence–Chemistry ; Biopolymers–Metabolism ; Gtp-Binding Proteins–Metabolism ; Glutamine–Metabolism ; Humans–Chemistry ; I-Kappa B Proteins–Metabolism ; Nf-Kappa B–Metabolism ; Transglutaminases–Metabolism ; Biopolymers ; I-Kappa B Proteins ; Nf-Kappa B ; Glutamine ; Transglutaminase 2 ; Transglutaminases ; Gtp-Binding Proteins
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descriptionRecently we reported that transglutaminase 2 (TGase 2) activates nuclear factor-kappaB (NF-kappaB) independently of I-kappaB kinase (IKK) activation, by inducing cross-linking and protein polymer formation of inhibitor of nuclear factor-kappaBalpha (I-kappaBalpha). TGase 2 catalyzes covalent isopeptide bond formation between the peptide bound-glutamine and the lysine residues. Using matrix-assisted laser desorption ionization time-of-flight mass spectra analysis of I-kappaBalpha polymers cross-linked by TGase 2, as well as synthetic peptides in an in vitro competition assay, we identified a glutamine cluster at the C terminus of I-kappaBalpha (amino acids 266-268) that appeared to play a key role in the formation of I-kappaBalpha polymers. Although there appeared to be no requirement for specific lysine residues, we found a considerably higher preference for the use of lysine residues at positions 21, 22, and 177 in TGase 2-mediated cross-linking of I-kappaBalpha. We demonstrated that synthetic peptides encompassing the glutamine cluster at amino acid positions 266-268 reversed I-kappaBalpha polymerization in vitro. Furthermore, the depletion of free I-kappaBalpha in EcR/TG cells was completely rescued in vivo by transfection of mutant I-kappaBalphas in glutamine sites (Q266G, Q267G, and Q313G) as well as in a lysine site (K177G). These findings provide additional clues into the mechanism by which TGase 2 contributes to the inflammatory process via activation of NF-kappaB.
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