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Gene Review

PELP1  -  proline, glutamate and leucine rich protein 1

Homo sapiens

Synonyms: HMX3, MNAR, Modulator of non-genomic activity of estrogen receptor, P160, Proline-, glutamic acid-and leucine-rich protein 1, ...
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Disease relevance of PELP1


High impact information on PELP1

  • These data reveal that MNAR mediates the crosstalk between two important classes of signal transducing molecules and suggest that ER "genomic" and "nongenomic" activities are interrelated [5].
  • We have identified a previously uncharacterized nuclear receptor-interacting protein designated as modulator of nongenomic activity of estrogen receptor (MNAR) [5].
  • We also show that MNAR, through activation of the Src/Erk phosphorylation cascade, affects ER transcriptional activity and ultimately ER-mediated gene expression [5].
  • A pine extensin-like protein (PELP) has been localized in metabolically active cells of differentiating xylem and in mature wood of loblolly pine (Pinus taeda L.). This proline-rich glycosylated protein was purified from cell walls of differentiating xylem by differential solubility and gel electrophoresis [6].
  • Functional implications of altered subcellular localization of PELP1 in breast cancer cells [7].

Chemical compound and disease context of PELP1


Biological context of PELP1


Anatomical context of PELP1


Associations of PELP1 with chemical compounds

  • The N-terminal leucine-abundant region of PELP1 was observed to interact with HDAC2 and exhibited repressive activity when tethered to the chromatin [10].
  • PELP1 (proline-, glutamic acid-, and leucine-rich protein-1) (also known as the modulator of nongenomic activity of estrogen receptor) plays a role in genomic functions of the estrogen receptor via histone interactions and in nongenomic functions via its influence on the MAPK-Src pathway [11].
  • In this study, we examined whether PELP1 expression is modulated by steroid hormone 17beta-estradiol (E2)-ER pathway [2].
  • We also found that E2 modulated PELP1 levels in an actinomycin-D-sensitive manner, suggesting transcriptional regulation [2].
  • PELP1 overexpression increased the micrococcal nuclease sensitivity of estrogen response element-containing nucleosomes [9].

Physical interactions of PELP1


Regulatory relationships of PELP1

  • The PELP1 promoter was similarly upregulated by both ERalpha and ERbeta and differentially regulated by selective estrogen receptor modulators in a cell line-dependent manner [2].
  • Mapping studies reveal that both the A/B domain and Y537 of ERalpha are required for MNAR-induced activation of ER transcriptional activity [14].
  • In conclusion, our results suggest that altered localization of PELP1 promotes heightened sensitivity to TNF-alpha in MCF-7 cells, paving the way for developing new treatment strategies for tumors with cytoplasmic PELP1 expression [15].

Other interactions of PELP1

  • The transcriptional corepressor, PELP1, recruits HDAC2 and masks histones using two separate domains [10].
  • PELP1 / MNAR staining was predominantly cytoplasmic whereas ER beta staining was nuclear and occasionally cytoplasmic in tumor cells [16].
  • Using mutant pRb cells, we demonstrated an essential role for PELP1/pRb interactions in the maximal coactivation functions of PELP1 using cyclin D1 as one of the targets [4].
  • Ligand stimulation promoted recruitment of PELP1 to 17beta-estradiol responsive promoters, its colocalization with acetylated H3, and increased PELP1-associated histone acetyltransferase enzymatic activity [9].
  • The primary structure of PELP1 consists of several motifs present in most transcriptional regulators including nine NR-interacting boxes (LXXLL motifs), a zinc finger, and glutamic acid- and proline-rich regions [12].

Analytical, diagnostic and therapeutic context of PELP1


  1. Deregulation of estrogen receptor coactivator proline-, glutamic acid-, and leucine-rich protein-1/modulator of nongenomic activity of estrogen receptor in human endometrial tumors. Vadlamudi, R.K., Balasenthil, S., Broaddus, R.R., Gustafsson, J.A., Kumar, R. J. Clin. Endocrinol. Metab. (2004) [Pubmed]
  2. Cloning and functional characterization of PELP1/MNAR promoter. Mishra, S.K., Balasenthil, S., Nguyen, D., Vadlamudi, R.K. Gene (2004) [Pubmed]
  3. Comprehensive Analysis of Recent Biochemical and Biologic Findings Regarding a Newly Discovered Protein-PELP1/MNAR. Rajhans, R., Vadlamudi, R.K. Clin. Exp. Metastasis (2006) [Pubmed]
  4. Functional interactions between the estrogen receptor coactivator PELP1/MNAR and retinoblastoma protein. Balasenthil, S., Vadlamudi, R.K. J. Biol. Chem. (2003) [Pubmed]
  5. Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade. Wong, C.W., McNally, C., Nickbarg, E., Komm, B.S., Cheskis, B.J. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  6. Wood contains a cell-wall structural protein. Bao, W., O'Malley, D.M., Sederoff, R.R. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  7. Functional implications of altered subcellular localization of PELP1 in breast cancer cells. Vadlamudi, R.K., Manavathi, B., Balasenthil, S., Nair, S.S., Yang, Z., Sahin, A.A., Kumar, R. Cancer Res. (2005) [Pubmed]
  8. Identifying the estrogen receptor coactivator PELP1 in autophagosomes. Ohshiro, K., Rayala, S.K., Kondo, S., Gaur, A., Vadlamudi, R.K., El-Naggar, A.K., Kumar, R. Cancer Res. (2007) [Pubmed]
  9. Potential role of a novel transcriptional coactivator PELP1 in histone H1 displacement in cancer cells. Nair, S.S., Mishra, S.K., Yang, Z., Balasenthil, S., Kumar, R., Vadlamudi, R.K. Cancer Res. (2004) [Pubmed]
  10. The transcriptional corepressor, PELP1, recruits HDAC2 and masks histones using two separate domains. Choi, Y.B., Ko, J.K., Shin, J. J. Biol. Chem. (2004) [Pubmed]
  11. Hepatocyte growth factor-regulated tyrosine kinase substrate (HRS) interacts with PELP1 and activates MAPK. Rayala, S.K., Hollander, P., Balasenthil, S., Molli, P.R., Bean, A.J., Vadlamudi, R.K., Wang, R.A., Kumar, R. J. Biol. Chem. (2006) [Pubmed]
  12. Molecular cloning and characterization of PELP1, a novel human coregulator of estrogen receptor alpha. Vadlamudi, R.K., Wang, R.A., Mazumdar, A., Kim, Y., Shin, J., Sahin, A., Kumar, R. J. Biol. Chem. (2001) [Pubmed]
  13. 9-cis-retinoic acid up-regulates expression of transcriptional coregulator PELP1, a novel coactivator of the retinoid X receptor alpha pathway. Singh, R.R., Gururaj, A.E., Vadlamudi, R.K., Kumar, R. J. Biol. Chem. (2006) [Pubmed]
  14. Characterization of the interactions of estrogen receptor and MNAR in the activation of cSrc. Barletta, F., Wong, C.W., McNally, C., Komm, B.S., Katzenellenbogen, B., Cheskis, B.J. Mol. Endocrinol. (2004) [Pubmed]
  15. Altered localization of a coactivator sensitizes breast cancer cells to tumor necrosis factor-induced apoptosis. Rayala, S.K., Mascarenhas, J., Vadlamudi, R.K., Kumar, R. Mol. Cancer Ther. (2006) [Pubmed]
  16. Novel estrogen receptor coactivator PELP1/MNAR gene and ERbeta expression in salivary duct adenocarcinoma: potential therapeutic targets. Vadlamudi, R.K., Balasenthil, S., Sahin, A.A., Kies, M., Weber, R.S., Kumar, R., El-Naggar, A.K. Hum. Pathol. (2005) [Pubmed]
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