NEDD8
NEDD8 (NEDD8 ubiquitin like modifier, Nedd-8) is a ubiquitin-like protein that is conjugated to a limited set of cellular proteins in a process called neddylation. It plays an important role in cell cycle control and embryogenesis. Browse Assay Genie's current range of NEDD8 research reagents below, or read on for the biology behind the target.
NEDD8 is a ubiquitin-like protein that acts by covalent attachment to a limited number of cellular proteins, notably cullins and p53/TP53. Attachment of NEDD8 to cullins is critical for the recruitment of E2 to the cullin-RING-based E3 ubiquitin-protein ligase complex. This facilitates polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins, which links neddylation to cell cycle control. Attachment of NEDD8 to p53/TP53 inhibits its transcriptional activity, and neddylation of EGFR results in protein stabilisation and translocation to the cell membrane.
Covalent attachment of NEDD8 to its substrates requires prior activation by the E1 complex UBE1C-APPBP1 and linkage to the E2 enzyme UBE2M. The NEDD8 protein belongs to the ubiquitin family and is annotated as localising to the nucleus. The NEDD8 gene is annotated as enabling ubiquitin protein ligase binding and as acting upstream of or within protein neddylation, with the protein located in the nucleoplasm.
The name derives from the earlier designation neural precursor cell expressed, developmentally down-regulated 8. NEDD8 has been reported as a biomarker of Parkinson's disease, alcohol-associated liver disease and malignant astrocytoma, which makes it of interest in studies of neurodegeneration, liver disease and cancer. Mouse and rat orthologs, both named Nedd8, are recognised, so the protein can be studied in common rodent models.
Neddylation of cullins supports degradation of cyclins and other regulatory proteins, making NEDD8 central to studies of cell cycle progression.
NEDD8 enables recruitment of E2 to cullin-RING E3 ligase complexes, a key step in polyubiquitination and proteasomal degradation.
Neddylation inhibits p53 transcriptional activity and stabilises EGFR at the cell membrane, relevant to tumour signalling research.
NEDD8 is reported as a biomarker of Parkinson's disease, alcohol-associated liver disease and malignant astrocytoma.
NEDD8 is a ubiquitin-like protein conjugated to a limited number of cellular proteins, including cullins and p53/TP53. Neddylation of cullins recruits E2 to cullin-RING E3 ligase complexes, promoting degradation of cyclins and other regulators, while neddylation of p53 inhibits its transcriptional activity.
NEDD8 is also written Nedd-8, and was previously named neural precursor cell expressed, developmentally down-regulated 8. Conjugation requires activation by the E1 complex UBE1C-APPBP1 and transfer to the E2 enzyme UBE2M before attachment to substrates.
Mouse and rat both have a Nedd8 ortholog, so rodent models are available for study; check the datasheet of any product for its validated reactivity. NEDD8 is reported as a biomarker of Parkinson's disease, alcohol-associated liver disease and malignant astrocytoma.
Other NEDD-named proteins and ubiquitin pathway targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q15843; product specifications from Assay Genie datasheets.