PRAME
PRAME (PRAME nuclear receptor transcriptional regulator, also known as CT130 and MAPE) is a tumour-associated antigen that acts as a substrate-recognition component of a Cul2-RING E3 ubiquitin ligase and as a repressor of retinoic acid receptor signalling. Browse Assay Genie's current range of PRAME research reagents below, or read on for the biology behind the target.
PRAME functions as the substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex, which mediates ubiquitination of target proteins and leads to their degradation. The CRL2(PRAME) complex targets truncated MSRB1/SEPX1 selenoproteins produced by failed UGA/Sec decoding. In the nucleus, the complex is recruited to epigenetically and transcriptionally active promoter regions bound by nuclear transcription factor Y (NFY), and probably plays a role in chromatin regulation.
PRAME also works as a transcriptional repressor. It inhibits retinoic acid signalling through the retinoic acid receptors RARA, RARB and RARG, and so prevents retinoic acid-induced cell proliferation arrest, differentiation and apoptosis. According to the NCBI Gene summary, this repressor activity likely confers a growth advantage to cancer cells. UniProt records the protein in the nucleus, chromosome, cytoplasm, Golgi apparatus and cell membrane, and places it in the PRAME family. The PRAME gene undergoes alternative splicing, which produces multiple transcript variants.
The name reflects its discovery as an antigen preferentially expressed in human melanomas, where it is recognised by cytolytic T lymphocytes; the previous name was preferentially expressed antigen in melanoma. It is not expressed in normal tissues except testis, a pattern that makes the PRAME protein a frequent subject in tumour immunology and cancer biology. Researchers working with a PRAME antibody or PRAME ELISA kit typically study its expression in tumour material and its role in retinoic acid pathway repression.
PRAME is preferentially expressed in human melanomas and is recognised by cytolytic T lymphocytes, making it a well-known tumour antigen.
PRAME represses signalling through RARA, RARB and RARG, blocking retinoic acid-induced growth arrest, differentiation and apoptosis.
As a substrate receptor of the CRL2 complex, PRAME directs ubiquitination and degradation of targets such as truncated MSRB1/SEPX1 selenoproteins.
The CRL2(PRAME) complex is recruited to active promoters bound by NFY and probably contributes to chromatin regulation.
PRAME is a substrate-recognition component of a Cul2-RING E3 ubiquitin ligase complex that mediates ubiquitination and degradation of target proteins. It also acts as a transcriptional repressor, inhibiting retinoic acid signalling through RARA, RARB and RARG and preventing retinoic acid-induced arrest, differentiation and apoptosis.
PRAME is also called CT130 and MAPE. UniProt lists the protein as melanoma antigen preferentially expressed in tumours, and an earlier name was preferentially expressed antigen in melanoma. HGNC now names the gene PRAME nuclear receptor transcriptional regulator. Alternative splicing gives multiple transcript variants.
PRAME is preferentially expressed in human melanomas and is recognised by cytolytic T lymphocytes. It is not expressed in normal tissues except testis. By repressing retinoic acid receptor signalling, it likely gives cancer cells a growth advantage. Check the datasheet of any product for its validated reactivity.
Retinoic acid receptors, CRL2 ubiquitin ligase components and selenoprotein substrates connected to PRAME biology.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P78395; product specifications from Assay Genie datasheets.