RNF125 mediated ubiquitination of RIG-I, MDA5 and IPS-1

Stable Identifier
R-NUL-936401
Type
Reaction [omitted]
Species
Mus musculus
Compartment
cytosol
ReviewStatus
5/5
General
SVG | 
PNG
Low
Medium
High
 | PPTX  | SBGN
RNF125 mediated ubiquitination of RIG-I, MDA5 and IPS-1
RNF125 acts as an E3-ubiquitin ligase that conjugates with RIG-I (DDX58), MDA5 (IFIH1) and IPS-1 (MAVS) and mediate their proteosomal degradation. UbcH1, UbcH5a, UbcH5b, and UbcH5c function as an E2 enzyme and conjugate ubiquitin to RNF125 and DDX58 via K48. Among these enzymes UbcH5c is the major E2 enzyme showing enhanced ubiquitin conjugation to DDX58. RNF125 mediated ubiquitination of RIG-I, MDA5 and MAVS (IPS-1) inhibits DDX58/IFIH1 signaling by shunting these proteins toward proteasomal degradation.
Literature References
PubMed ID Title Journal Year
17460044 Negative regulation of the RIG-I signaling by the ubiquitin ligase RNF125

Arimoto, K, Fujita, T, Hishiki, T, Shimotohno, K, Takahashi, H, Konishi, H

Proc Natl Acad Sci U S A 2007
Participants
Input
Output
Catalyst Activity

ubiquitin-protein transferase activity of Rnf125:E2 enzyme (UBE2K, UbcH5a-c):K48-polyubiquitin [cytosol]

Physical Entity
Rnf125:E2 enzyme (UBE2K, UbcH5a-c):K48-polyubiquitin [cytosol] (Mus musculus)
Activity
ubiquitin-protein transferase activity (GO:0004842)
Orthologous Events
RNF125 mediated ubiquitination of DDX58, IFIH1 and MAVS (Homo sapiens)
Authored
Garapati, P V  (2010-08-23)
Reviewed
Akira, S  (2010-10-30)
Kawai, T  (2010-10-30)
Created
Garapati, P V  (2010-08-23)
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