TRIM9
TRIM9 (tripartite motif containing 9, also known as SPRING or RNF91) is an E3 ubiquitin-protein ligase of the TRIM/RBCC family. It ubiquitinates itself and other substrates, and has been linked to filopodial dynamics, neuronal function and synaptic vesicle exocytosis. Browse Assay Genie's current range of TRIM9 research reagents below, or read on for the biology behind the target.
TRIM9 is an E3 ubiquitin-protein ligase. Working with the E2 enzyme UBE2D2 (UBC4), it ubiquitinates itself, and this modification serves as a targeting signal for proteasomal degradation. In the brain, TRIM9 regulates filopodial dynamics by promoting the ubiquitination and degradation of the actin polymerase VASP. This activity is antagonised by TRIM67. TRIM9 may also act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25 for SNARE complex formation.
The TRIM9 gene encodes a member of the tripartite motif (TRIM) family, which belongs to the wider RBCC group. The TRIM motif comprises three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, followed by a coiled-coil region. HGNC places TRIM9 among the RING finger E3 ubiquitin protein ligases and among fibronectin type III domain containing proteins. In UniProt, the TRIM9 protein is annotated in the cytoplasm, the cytoskeleton, dendrites, synapses and synaptic vesicles, and NCBI Gene reports localisation to cytoplasmic bodies. Alternative splicing of the gene produces two transcript variants that encode different isoforms.
TRIM9 may play a role in regulating neuronal functions. It may also take part in the formation or breakdown of abnormal inclusions in neurodegenerative disorders. The gene has also been called SPRING and RNF91, and HGNC records the previous name tripartite motif-containing 9. Mouse and rat both carry a Trim9 ortholog.
TRIM9 may regulate neuronal functions, and it localises to dendrites and synapses, making it a relevant target for studying neuronal cell biology.
TRIM9 is a RING-type E3 ligase that works with UBE2D2 and self-ubiquitinates as a signal for proteasomal degradation.
TRIM9 promotes ubiquitination and degradation of VASP to regulate filopodial dynamics in brain, an activity antagonised by TRIM67.
TRIM9 may control the availability of SNAP25 for SNARE complex formation, linking it to the regulation of synaptic vesicle exocytosis.
TRIM9 is an E3 ubiquitin-protein ligase that ubiquitinates itself with the E2 enzyme UBE2D2, marking it for proteasomal degradation. It promotes VASP ubiquitination and degradation to regulate filopodial dynamics in brain, and may regulate synaptic vesicle exocytosis through SNAP25.
TRIM9 is also known as SPRING and RNF91, and its former HGNC name was tripartite motif-containing 9. UniProt names the protein E3 ubiquitin-protein ligase TRIM9. NCBI Gene reports that alternative splicing generates two transcript variants encoding different isoforms.
Mouse and rat both have a Trim9 ortholog. UniProt notes that TRIM9 may take part in the formation or breakdown of abnormal inclusions in neurodegenerative disorders, though this is described as a possible role. Check the datasheet of any product for its validated reactivity.
Other members of the TRIM family of RING-type E3 ubiquitin ligases with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9C026; product specifications from Assay Genie datasheets.