Format

Send to

Choose Destination
See comment in PubMed Commons below
J Cell Biol. 2007 Apr 23;177(2):265-75.

The interaction between the ER membrane protein UNC93B and TLR3, 7, and 9 is crucial for TLR signaling.

Author information

  • 1Whitehead Institute for Biomedical Research, Cambridge, MA 02142.

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.

PMID:
17452530
PMCID:
PMC2064135
DOI:
10.1083/jcb.200612056
[PubMed - indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Support Center