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topographic separation of the presynaptic terminals of adjacent nociceptive neurons requires different levels of Trim9, an evolutionarily conserved signaling molecule
TRIM9s undergoes Lys (show LYZ Proteins)-63-linked auto-polyubiquitination and serves as a platform to bridge GSK3beta to TBK1 (show TBK1 Proteins), leading to the activation of IRF3 (show IRF3 Proteins) signaling.
Authors demonstrate that tripartite motif protein 9 (TRIM9)-dependent ubiquitination of DCC (show DCC Proteins) blocks the interaction with and phosphorylation of FAK (show PTK2 Proteins).
TRIM9 is a brain-specific (show CALY Proteins) negative regulator of the NF-kappaB (show NFKB1 Proteins) pro-inflammatory signalling pathway.
These results suggest that TRIM9 plays an important role in the regulation of neuronal functions and participates in pathological process of Lewy body disease through its ligase activity.
Trim9 mediates cellular movement and migration in macrophages as well as neurons.
Adult-born dentate granule cells lacking Trim9 exhibited excessive dendritic arborization and mislocalization of cell bodies in vivo
a gradient of TRIM9-mediated ubiquitination of VASP (show VASP Proteins) creates a filopodial stability gradient during axon turning
TRIM9 is expressed in the mouse embryonic and adult nervous system
The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes to cytoplasmic bodies. Its function has not been identified. Alternate splicing of this gene generates two transcript variants encoding different isoforms.
tripartite motif-containing 9
, tripartite motif containing 9
, anomalies in sensory axon patterning
, tripartite motif protein 9
, E3 ubiquitin-protein ligase TRIM9
, RING finger protein 91
, homolog of rat RING finger Spring
, tripartite motif-containing protein 9
, SNAP-25-interacting RING finger protein