{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPELP1 is a multifunctional scaffold protein endowed with multiple interaction motifs—most notably nine LXXLL boxes—that enable it to serve as a coregulator of nuclear hormone receptors such as estrogen receptor α (ERα). In its canonical role, PELP1 facilitates ligand‐dependent transcription by recruiting general coactivators and chromatin‐modifying enzymes, thereby modulating histone acetylation, methylation, and ultimately chromatin remodeling. In addition, interactions with key cell cycle regulators, including the retinoblastoma protein (pRb), underscore its importance in cell cycle progression and gene regulation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its nuclear functions, PELP1 acts as a critical adaptor in extranuclear signaling, bridging steroid receptors with key cytoplasmic kinases. It participates in non‐genomic pathways by interacting with proteins such as Src, c‐Src–dependent MAPK effectors, PI3K/AKT, and mTOR. Growth factor–induced phosphorylation—mediated in part by PKA—modulates its subcellular trafficking, and altered (cytoplasmic) localization has been linked to increased estrogen sensitivity, resistance to antiestrogens like tamoxifen, and the acquisition of aggressive, stem cell–like properties. Moreover, partnerships with other coactivators such as SRC-3/AIB1 and transcription factors like TFAP2C amplify its role in integrating hormonal and growth factor signals."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to modulating transcription factor activity at promoters, PELP1 helps reprogram the epigenetic landscape by engaging histone demethylases such as KDM1 and arginine methyltransferases like CARM1—mechanisms that shift histone methylation marks at target genes. Genome‐wide analyses have further revealed a role for PELP1 in regulating alternative splicing of oncogenic transcripts. Moreover, within the nucleolus, PELP1 is an integral component of complexes that include TEX10, WDR18, and the AAA ATPase MDN1; through a SUMO‐regulated cycle, these interactions are essential for the maturation and nucleolar release of pre–60S ribosomal subunits."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDeregulation and overexpression of PELP1 have been implicated in the oncogenesis and progression of a broad spectrum of malignancies—including breast, ovarian, endometrial, prostate, lung, and astrocytic tumors. Aberrant subcellular distribution, particularly cytoplasmic mislocalization, has been associated with enhanced metastasis, therapy resistance, and poorer clinical outcomes. PELP1 contributes to tumor progression by (a) modulating the expression of metastasis‐suppressing microRNAs; (b) upregulating aromatase expression, thereby contributing to local (in situ) estrogen synthesis and autocrine proliferative loops; and (c) sustaining oncogenic signaling networks that drive cell survival, proliferation, and genomic instability. Collectively, these findings highlight PELP1’s pivotal role as an oncogene that integrates hormonal signals and growth factor pathways to foster aggressive tumor behavior."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "18", "end_ref": "34"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "R K Vadlamudi, R A Wang, A Mazumdar, et al. 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