TRIM3
TRIM3 (tripartite motif containing 3, also known as HAC1, BERP, RNF97 and RNF22) is a RING-type E3 ubiquitin ligase of the TRIM family. It supports neuronal plasticity, learning and memory, and also contributes to innate immunity and cell cycle regulation. Browse Assay Genie's current range of TRIM3 research reagents below, or read on for the biology behind the target.
TRIM3 is an E3 ubiquitin ligase with essential roles in neuronal functions, including the regulation of neuronal plasticity, learning and memory. In neurons it is a component of a cytoskeleton-associated recycling or transport complex, where it polyubiquitinates gamma-actin. It also ubiquitinates the postsynaptic scaffold protein GKAP, a substrate involved in synaptic remodelling, and so modulates dendritic spine morphology. In addition, it positively regulates the motility of the microtubule-dependent motor protein KIF21B.
Beyond the nervous system, TRIM3 takes part in innate immunity and cell cycle regulation. Through its RING-dependent E3 ligase activity it induces growth arrest and ubiquitinates CDKN1A. It positively regulates TLR3-mediated signalling by mediating 'Lys-63'-linked polyubiquitination of TLR3, which in turn promotes the recognition and sorting of polyubiquitinated TLR3 by the ESCRT complexes.
The TRIM3 protein belongs to the tripartite motif (TRIM) family, also called the RING-B-box-coiled-coil (RBCC) subgroup of RING finger proteins. The TRIM motif combines three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, with a coiled-coil region. The protein localises to cytoplasmic filaments, and is also found in early endosomes, the trans-Golgi network and dendrites. The human protein is similar to a rat protein that binds the tail domain of myosin V and can interact with alpha-actinin-4, which suggests a role in myosin V-mediated cargo transport. The TRIM3 gene has mouse and rat orthologs, both named Trim3, and alternatively spliced transcript variants encode the same isoform.
TRIM3 polyubiquitinates gamma-actin in a neuronal transport complex, regulating plasticity, learning and memory.
By ubiquitinating the scaffold GKAP, TRIM3 modulates dendritic spine morphology and synaptic remodelling.
TRIM3 promotes Lys-63-linked polyubiquitination of TLR3 and its ESCRT-mediated sorting, positively regulating TLR3 signalling.
RING-dependent E3 activity of TRIM3 induces growth arrest and ubiquitinates CDKN1A, linking it to cell cycle control.
TRIM3 is an E3 ubiquitin ligase. In neurons it polyubiquitinates gamma-actin and GKAP, influencing plasticity, learning, memory and dendritic spine morphology. It also ubiquitinates CDKN1A to induce growth arrest and promotes TLR3 signalling through Lys-63-linked polyubiquitination.
TRIM3, or tripartite motif containing 3, has the aliases and previous symbols HAC1, BERP, RNF97 and RNF22. The previous name was tripartite motif-containing 3. HGNC places it among RING finger proteins, the tripartite motif family and RING finger E3 ubiquitin protein ligases.
Yes. Mouse and rat both have a Trim3 ortholog. A rat protein similar to human TRIM3 binds the tail domain of myosin V and interacts with alpha-actinin-4. Check the datasheet of any product for its validated reactivity.
Other TRIM family E3 ubiquitin ligases with related RING, B-box and coiled-coil architecture, with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt O75382; product specifications from Assay Genie datasheets.