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Identification of interaction sites for dimerization and adapter recruitment in Toll/interleukin-1 receptor (TIR) domain of Toll-like receptor 4

Celia Bovijn UGent, Peter Ulrichts UGent, Anne-Sophie De Smet UGent, Dominiek Catteeuw UGent, Rudi Beyaert UGent, Jan Tavernier UGent and Frank Peelman UGent (2012) JOURNAL OF BIOLOGICAL CHEMISTRY. 287(6). p.4088-4098
abstract
Toll-like receptor signaling requires interactions of the Toll/IL-1 receptor (TIR) domains of the receptor and adapter proteins. Using the mammalian protein-protein interaction trap strategy, homology modeling, and site-directed mutagenesis, we identify the interaction surfaces in the TLR4 TIR domain for the TLR4-TLR4, TLR4-MyD88 adapter-like (MAL), and TLR4-TRIF-related adapter molecule (TRAM) interaction. Two binding sites are equally important for TLR4 dimerization and adapter recruitment. In a model based on the crystal structure of the dimeric TLR10 TIR domain, the first binding site mediates TLR4-TLR4 TIR-TIR interaction. Upon dimerization, two identical second binding sites of the TLR4 TIR domain are juxtaposed and form an extended binding platform for both MAL and TRAM. In our mammalian protein-protein interaction trap assay, MAL and TRAM compete for binding to this platform. Our data suggest that adapter binding can stabilize the TLR4 TIR dimerization.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
TLR4, DIMER, ACTIVATION, PROTEINS, STRUCTURAL BASIS, INTERACTION TRAP, CRYSTAL-STRUCTURE, SIGNAL-TRANSDUCTION, MULTIPLE SEQUENCE ALIGNMENT, NF-KAPPA-B
journal title
JOURNAL OF BIOLOGICAL CHEMISTRY
J. Biol. Chem.
volume
287
issue
6
pages
4088 - 4098
Web of Science type
Article
Web of Science id
000300410900042
JCR category
BIOCHEMISTRY & MOLECULAR BIOLOGY
JCR impact factor
4.651 (2012)
JCR rank
61/288 (2012)
JCR quartile
1 (2012)
ISSN
0021-9258
DOI
10.1074/jbc.M111.282350
project
Ghent researchers on unfolded proteins in inflammatory disease (GROUP-ID)
project
Ghent researchers on unfolded proteins in inflammatory disease (GROUP-ID)
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
2083527
handle
http://hdl.handle.net/1854/LU-2083527
date created
2012-04-11 13:39:23
date last changed
2014-05-12 10:59:13
@article{2083527,
  abstract     = {Toll-like receptor signaling requires interactions of the Toll/IL-1 receptor (TIR) domains of the receptor and adapter proteins. Using the mammalian protein-protein interaction trap strategy, homology modeling, and site-directed mutagenesis, we identify the interaction surfaces in the TLR4 TIR domain for the TLR4-TLR4, TLR4-MyD88 adapter-like (MAL), and TLR4-TRIF-related adapter molecule (TRAM) interaction. Two binding sites are equally important for TLR4 dimerization and adapter recruitment. In a model based on the crystal structure of the dimeric TLR10 TIR domain, the first binding site mediates TLR4-TLR4 TIR-TIR interaction. Upon dimerization, two identical second binding sites of the TLR4 TIR domain are juxtaposed and form an extended binding platform for both MAL and TRAM. In our mammalian protein-protein interaction trap assay, MAL and TRAM compete for binding to this platform. Our data suggest that adapter binding can stabilize the TLR4 TIR dimerization.},
  author       = {Bovijn, Celia and Ulrichts, Peter and De Smet, Anne-Sophie and Catteeuw, Dominiek and Beyaert, Rudi and Tavernier, Jan and Peelman, Frank},
  issn         = {0021-9258},
  journal      = {JOURNAL OF BIOLOGICAL CHEMISTRY},
  keyword      = {TLR4,DIMER,ACTIVATION,PROTEINS,STRUCTURAL BASIS,INTERACTION TRAP,CRYSTAL-STRUCTURE,SIGNAL-TRANSDUCTION,MULTIPLE SEQUENCE ALIGNMENT,NF-KAPPA-B},
  language     = {eng},
  number       = {6},
  pages        = {4088--4098},
  title        = {Identification of interaction sites for dimerization and adapter recruitment in Toll/interleukin-1 receptor (TIR) domain of Toll-like receptor 4},
  url          = {http://dx.doi.org/10.1074/jbc.M111.282350},
  volume       = {287},
  year         = {2012},
}

Chicago
Bovijn, Celia, Peter Ulrichts, Anne-Sophie De Smet, Dominiek Catteeuw, Rudi Beyaert, Jan Tavernier, and Frank Peelman. 2012. “Identification of Interaction Sites for Dimerization and Adapter Recruitment in Toll/interleukin-1 Receptor (TIR) Domain of Toll-like Receptor 4.” Journal of Biological Chemistry 287 (6): 4088–4098.
APA
Bovijn, C., Ulrichts, P., De Smet, A.-S., Catteeuw, D., Beyaert, R., Tavernier, J., & Peelman, F. (2012). Identification of interaction sites for dimerization and adapter recruitment in Toll/interleukin-1 receptor (TIR) domain of Toll-like receptor 4. JOURNAL OF BIOLOGICAL CHEMISTRY, 287(6), 4088–4098.
Vancouver
1.
Bovijn C, Ulrichts P, De Smet A-S, Catteeuw D, Beyaert R, Tavernier J, et al. Identification of interaction sites for dimerization and adapter recruitment in Toll/interleukin-1 receptor (TIR) domain of Toll-like receptor 4. JOURNAL OF BIOLOGICAL CHEMISTRY. 2012;287(6):4088–98.
MLA
Bovijn, Celia, Peter Ulrichts, Anne-Sophie De Smet, et al. “Identification of Interaction Sites for Dimerization and Adapter Recruitment in Toll/interleukin-1 Receptor (TIR) Domain of Toll-like Receptor 4.” JOURNAL OF BIOLOGICAL CHEMISTRY 287.6 (2012): 4088–4098. Print.