LRR FLII-interacting protein 1 binds dsDNA

Stable Identifier
R-HSA-3134896
Type
Reaction [binding]
Species
Homo sapiens
Related Species
Hepatitis C Virus
Compartment
cytosol
ReviewStatus
5/5
Locations in the PathwayBrowser
Expand all
General
SVG | 
PNG
Low
Medium
High
 | PPTX  | SBGN
LRR FLII-interacting protein 1 binds dsDNA
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
LRRFIP1 can recognize both AT-rich B-form dsDNA and GC-rich Z-form dsDNA (Yang P et al. 2010). Induction of IFN-beta by LRRFIP1 was enhanced with the presence of hepatitis C virus (Liu Y et al. 2015). Overexpression of LRRFIP1 in hepatocyte derived cellular carcinoma cell lines (Huh7 and Huh7.5.1) inhibited HCV replication. However, HCV infection did not regulate intracellular expression of LRRFIP1 (Liu Y et al. 2015). In addition, the C-terminus of LRRFIP1 has been described as having nucleic acid-binding activity, including the transactivating response region (TAR) hairpin of HIV (Liu YT & Yin HL 1998; Choe N et al. 2013). Moreover, LRRFIP1 induced type I IFNs in 3T3 cells in the presence of influenza virus and contributed to the production of IFN-beta in mouse macrophages induced by VSV (vesicular stomatitis virus) and Listeria monocytogenes (Bagashev A et al. 2010; Yang P et al. 2010).

LRRFIP1 contains three domains, an N-terminal helical region of unknown function, a central coiled coil (CC) domain that interacts with protein flightless I homolog (FLII), and a C-terminal DNA binding or nucleic acid recognition domain (DBD). The structural and biophysical studies revealed that the CC-domain of LRRFIP1 forms stable homodimer in solution while the CC-DBD construct was found to be an oligomer suggesting that the full length LRRFIP1 may also form dimers or larger oligomers upon DNA binding (Nguyen JB and Modis Y 2012).

Literature References
PubMed ID Title Journal Year
23099021 Crystal structure of the dimeric coiled-coil domain of the cytosolic nucleic acid sensor LRRFIP1

Nguyen, JB, Modis, Y

J. Struct. Biol. 2013
20453844 The cytosolic nucleic acid sensor LRRFIP1 mediates the production of type I interferon via a beta-catenin-dependent pathway

Yang, P, An, H, Liu, X, Wen, M, Zheng, Y, Rui, Y, Cao, X

Nat. Immunol. 2010
Participants
Input
Output
Participates
as an event of
Authored
Shamovsky, V  (2013-02-06)
Reviewed
D'Eustachio, P  (2013-02-11)
Jin, L  (2013-05-22)
Wu, J  (2013-05-22)
Created
Shamovsky, V  (2013-02-13)
Cite Us!