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topographic separation of the presynaptic terminals of adjacent nociceptive neurons requires different levels of Trim9, an evolutionarily conserved signaling molecule
Authors demonstrate that tripartite motif protein 9 (TRIM9)-dependent ubiquitination of DCC (Montrer DCC Kits ELISA) blocks the interaction with and phosphorylation of FAK (Montrer PTK2 Kits ELISA).
TRIM9 is a brain-specific (Montrer CALY Kits ELISA) negative regulator of the NF-kappaB (Montrer NFKB1 Kits ELISA) 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.
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 (Montrer VASP Kits ELISA) 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