Proline, glutamic acid, and leucine rich protein 1 (PELP1) is a large multi-domain protein that has been shown to modulate an increasing number of pathways and biological processes. The first reports describing the cloning and characterization of PELP1 showed that it was an estrogen receptor coactivator. PELP1 has now been shown to be a coregulator for a growing number of transcription factors. Furthermore, recent reports have shown that PELP1 is a member of chromatin remodeling complexes. In addition to PELP1 nuclear functions, it has been shown to have cytoplasmic signaling functions as well. In the cytoplasm PELP1 acts as a scaffold molecule and mediates rapid signaling from growth factor and hormone receptors. PELP1 signaling ultimately plays a role in cancer biology by increasing proliferation and metastasis, among other cellular processes. Here we will review (1) the cloning and characterization of PELP1 expression, (2) interacting proteins, (3) PELP1 signaling, and (4) PELP1-mediated biology.
Keywords: AIB1; AR; BCAS3; CBP; CREB binding protein; ChIP; Coactivator; E2; ER; ERRα; Estrogen signaling; Extra-nuclear signaling; FHL2; GR; HDAC; Hormone resistance; IHC; ILK1; KDM1; LIM domain; Lin-1, Isl-1, and Mec-3 domain; MNAR; Modulator of Nongenomic Activity of ER; PELP1; RXR; SH2; SH3; STAT3; TIF2; amplified in breast cancer 1; androgen receptor; breast carcinoma amplified sequence 3; c-Src homology domain 2; c-Src homology domain 3; chromatin immunoprecipitation; estradiol; estrogen receptor; estrogen-related receptor alpha; four and a half LIM domains 2; glucocorticoid receptor; histone deacetylase; immunohistochemistry; integrin-linked kinase 1; lysine-specific histone demethylase 1; proline, glutamic acid and leucine rich protein 1; retinoid X receptor; signal transducer and activator or transcription 3; transcriptional mediators/intermediary factor 2.
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