PELP1
PELP1 (proline-, glutamic acid- and leucine-rich protein 1, also known as MNAR) is a scaffold-like coregulator that coactivates oestrogen receptor-mediated transcription and corepresses other nuclear hormone receptors and sequence-specific transcription factors. It also acts in ribosome biogenesis. Browse Assay Genie's current range of PELP1 research reagents below, or read on for the biology behind the target.
PELP1 coactivates oestrogen receptor (ER)-mediated transcription and corepresses genes driven by other nuclear hormone receptors and sequence-specific transcription factors. When present in the nucleus, it contributes to ER genomic activity by activating ER target genes in a manner that depends on hormonal stimulation. In the cytosol, it can facilitate ER non-genomic signalling through interaction with SRC and PI3K. It also contributes to E2-mediated cell cycle progression by interacting with RB1, and it may have functional implications in ER and growth factor cross-talk, including interactions with signalling components such as EGFR and HRS.
Beyond hormone signalling, PELP1 has roles in chromatin-associated and nucleolar processes. It is the key stabilising component of the Five Friends of Methylated CHTOP (5FMC) complex, which is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and transactivation of its target genes. It is also part of the PELP1 complex involved in the nucleolar steps of 28S rRNA maturation and the nucleoplasmic transit of the pre-60S ribosomal subunit, where it regulates pre-60S association of the remodelling factor MDN1. UniProt places it in the RIX1/PELP1 family, and HGNC groups the PELP1 gene with the large ribosomal subunit biogenesis complex and armadillo-like helical domain-containing proteins.
PELP1 is localised to the nucleolus, nucleoplasm and cytoplasm. According to the NCBI Gene summary, its expression is regulated by both members of the oestrogen receptor family, and alternative splicing yields multiple transcript variants. The protein may promote tumorigenesis through interaction with and modulation of oncogenes including SRC, PI3K, STAT3 and EGFR, and it may influence cancer cell metastasis by modulating E2-mediated cytoskeleton changes and cell migration. Previous HGNC names and symbols include MNAR and proline, glutamic acid and leucine rich protein 1.
PELP1 coactivates ER target genes and links nuclear and cytosolic ER signalling through SRC and PI3K, making it a focus for hormone-response studies.
PELP1 may promote tumorigenesis by modulating oncogenes such as SRC, PI3K, STAT3 and EGFR, and may be involved in progression of several cancer types.
As part of the PELP1 complex, it acts in 28S rRNA maturation and pre-60S transit, and regulates pre-60S association of MDN1.
PELP1 stabilises the 5FMC complex, which drives desumoylation of ZNF148 and transactivation of its targets, and corepresses other transcription factors.
PELP1 coactivates oestrogen receptor-mediated transcription and corepresses other nuclear hormone receptors and transcription factors. It can also support ER non-genomic signalling via SRC and PI3K in the cytosol, and it takes part in nucleolar 28S rRNA maturation and pre-60S ribosomal subunit transit.
Yes. MNAR is an alias and previous symbol for PELP1. The earlier HGNC name was proline, glutamic acid and leucine rich protein 1, and the current approved name is proline, glutamate and leucine rich protein 1. Alternative splicing of the gene produces multiple transcript variants.
The data list mouse and rat orthologs, both named Pelp1. PELP1 may be involved in the progression of several cancer types, possibly via SRC, PI3K, STAT3 and EGFR. Check the datasheet of any product for its validated reactivity.
Estrogen receptors, signalling kinases, oncogenic partners and ribosome biogenesis factors related to PELP1 with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q8IZL8; product specifications from Assay Genie datasheets.