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The interaction between the er membrane protein unc93b and tlr3, 7, and 9 is crucial for tlr signaling

Academic Article
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Overview

authors

  • Brinkmann, M. M.
  • Spooner, E.
  • Hoebe, K.
  • Beutler, Bruce
  • Ploegh, H. L.
  • Kim, Y. M.

publication date

  • April 2007

journal

  • Journal of Cell Biology  Journal

abstract

  • Toll-like receptors (TLRs) sense the presence of microbial and viral pathogens by signal transduction mechanisms that remain to be fully elucidated. A single point mutation (H412R) in the polytopic endoplasmic reticulum (ER)-resident membrane protein UNC93B abolishes signaling via TLR3, 7, and 9. We show that UNC93B specifically interacts with TLR3, 7, 9, and 13, whereas introduction of the point mutation H412R in UNC93B abolishes their interactions. We establish the physical interaction of the intracellular TLRs with UNC93B in splenocytes and bone marrow-derived dendritic cells. Further, by expressing chimeric TLRs, we show that TLR3 and 9 bind to UNC93B via their transmembrane domains. We propose that a physical association between UNC93B and TLRs in the ER is essential for proper TLR signaling.

subject areas

  • Amino Acid Substitution
  • Animals
  • Bone Marrow Cells
  • Cell Line
  • Endoplasmic Reticulum
  • Humans
  • Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
  • Membrane Glycoproteins
  • Membrane Transport Proteins
  • Mice
  • Mice, Inbred C57BL
  • Molecular Sequence Data
  • Point Mutation
  • Signal Transduction
  • Spleen
  • Toll-Like Receptor 3
  • Toll-Like Receptor 7
  • Toll-Like Receptor 9
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Identity

PubMed Central ID

  • PMC2064135

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.200612056

PubMed ID

  • 17452530
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Additional Document Info

start page

  • 265

end page

  • 275

volume

  • 177

issue

  • 2

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