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Gene Review

Med1  -  mediator complex subunit 1

Mus musculus

Synonyms: AI480703, CRSP210, Crsp210, DRIP205, Drip205, ...
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High impact information on Pparbp


Biological context of Pparbp


Anatomical context of Pparbp

  • PPARgamma and PBP are expressed in the transitional epithelium of urinary bladder and in brown adipose tissue, but not SRC-1 [3].
  • In the colonic mucosa, PPARgamma expression occurs throughout the villi, whereas the expression of both SRC-1 and PBP is confined mostly to the crypts [3].
  • Deletion of PBP/PPARBP, the gene for nuclear receptor coactivator peroxisome proliferator-activated receptor-binding protein, results in embryonic lethality [7].
  • Disruption of the PBP/TRAP220 gene results in embryonic lethality around embryonic day 11.5 by affecting placental, cardiac, hepatic, and bone marrow development [6].
  • In contrast, scattered PBP(+/+) hepatocytes in these livers showed DNA synthesis and were markedly hypertrophic with peroxisome proliferation in response to PPARalpha ligands [6].

Associations of Pparbp with chemical compounds

  • Distinct roles of the steroid receptor coactivator 1 and of MED1 in retinoid-induced transcription and cellular differentiation [8].
  • The TRAP220 component of the TRAP/SMCC complex, a mammalian homologof the yeast Mediator that shows diverse coactivation functions, interacts directly with nuclear receptors [2].
  • Both the mammary ductal elongation in response to estrogen treatment and the mammary lobuloalveolar proliferation stimulated by estrogen plus progesterone were attenuated in PBP-deficient mammary glands [9].
  • Glimepiride enhanced the recruitment of coactivator DRIP205 and dissociation of corepressors such as nuclear receptor corepressor and silencing mediator for retinoid and thyroid hormone receptors [10].
  • Furthermore, flow cytometric analyses showed that HL-60 cells, human promyelocytic leukemia cell line, wherein TRAP220 was down-regulated, did not differentiate efficiently into monocytes and granulocytes by stimulation with 1,25-dihydroxyvitamin D(3) and all-trans retinoic acid, correspondingly [11].

Other interactions of Pparbp


Analytical, diagnostic and therapeutic context of Pparbp


  1. Thyroid hormone-induced juxtaposition of regulatory elements/factors and chromatin remodeling of Crabp1 dependent on MED1/TRAP220. Park, S.W., Li, G., Lin, Y.P., Barrero, M.J., Ge, K., Roeder, R.G., Wei, L.N. Mol. Cell (2005) [Pubmed]
  2. Involvement of the TRAP220 component of the TRAP/SMCC coactivator complex in embryonic development and thyroid hormone action. Ito, M., Yuan, C.X., Okano, H.J., Darnell, R.B., Roeder, R.G. Mol. Cell (2000) [Pubmed]
  3. Differential expression of the peroxisome proliferator-activated receptor gamma (PPARgamma) and its coactivators steroid receptor coactivator-1 and PPAR-binding protein PBP in the brown fat, urinary bladder, colon, and breast of the mouse. Jain, S., Pulikuri, S., Zhu, Y., Qi, C., Kanwar, Y.S., Yeldandi, A.V., Rao, M.S., Reddy, J.K. Am. J. Pathol. (1998) [Pubmed]
  4. Targeted disruption of the synovial sarcoma-associated SS18 gene causes early embryonic lethality and affects PPARBP expression. de Bruijn, D.R., Peters, W.J., Chuva de Sousa Lopes, S.M., van Dijk, A.H., Willemse, M.P., Pfundt, R., de Boer, P., Geurts van Kessel, A. Hum. Mol. Genet. (2006) [Pubmed]
  5. Transcriptional coactivator PRIP, the peroxisome proliferator-activated receptor gamma (PPARgamma)-interacting protein, is required for PPARgamma-mediated adipogenesis. Qi, C., Surapureddi, S., Zhu, Y.J., Yu, S., Kashireddy, P., Rao, M.S., Reddy, J.K. J. Biol. Chem. (2003) [Pubmed]
  6. Transcription coactivator PBP, the peroxisome proliferator-activated receptor (PPAR)-binding protein, is required for PPARalpha-regulated gene expression in liver. Jia, Y., Qi, C., Kashireddi, P., Surapureddi, S., Zhu, Y.J., Rao, M.S., Le Roith, D., Chambon, P., Gonzalez, F.J., Reddy, J.K. J. Biol. Chem. (2004) [Pubmed]
  7. Deletion of PBP/PPARBP, the gene for nuclear receptor coactivator peroxisome proliferator-activated receptor-binding protein, results in embryonic lethality. Zhu, Y., Qi, C., Jia, Y., Nye, J.S., Rao, M.S., Reddy, J.K. J. Biol. Chem. (2000) [Pubmed]
  8. Distinct roles of the steroid receptor coactivator 1 and of MED1 in retinoid-induced transcription and cellular differentiation. Flajollet, S., Lefebvre, B., Rachez, C., Lefebvre, P. J. Biol. Chem. (2006) [Pubmed]
  9. Peroxisome proliferator-activated receptor-binding protein null mutation results in defective mammary gland development. Jia, Y., Qi, C., Zhang, Z., Zhu, Y.T., Rao, S.M., Zhu, Y.J. J. Biol. Chem. (2005) [Pubmed]
  10. Sulfonylurea agents exhibit peroxisome proliferator-activated receptor gamma agonistic activity. Fukuen, S., Iwaki, M., Yasui, A., Makishima, M., Matsuda, M., Shimomura, I. J. Biol. Chem. (2005) [Pubmed]
  11. The role of transcriptional coactivator TRAP220 in myelomonocytic differentiation. Urahama, N., Ito, M., Sada, A., Yakushijin, K., Yamamoto, K., Okamura, A., Minagawa, K., Hato, A., Chihara, K., Roeder, R.G., Matsui, T. Genes Cells (2005) [Pubmed]
  12. The thyroid hormone receptor-associated protein TRAP220 is required at distinct embryonic stages in placental, cardiac, and hepatic development. Landles, C., Chalk, S., Steel, J.H., Rosewell, I., Spencer-Dene, B., Lalani, e.l.-.N., Parker, M.G. Mol. Endocrinol. (2003) [Pubmed]
  13. The different effects of endocrine-disrupting chemicals on estrogen receptor-mediated transcription through interaction with coactivator TRAP220 in uterine tissue. Inoshita, H., Masuyama, H., Hiramatsu, Y. J. Mol. Endocrinol. (2003) [Pubmed]
  14. Comparative distribution of the mammalian mediator subunit thyroid hormone receptor-associated protein (TRAP220) mRNA in developing and adult rodent brain. Galeeva, A., Treuter, E., Tuohimaa, P., Pelto-Huikko, M. Eur. J. Neurosci. (2002) [Pubmed]
  15. Regulation of Aurora-A kinase gene expression via GABP recruitment of TRAP220/MED1. Udayakumar, T.S., Belakavadi, M., Choi, K.H., Pandey, P.K., Fondell, J.D. J. Biol. Chem. (2006) [Pubmed]
  16. Purification and crystallization of the heterodimeric complex of RARbeta and RXRalpha ligand-binding domains in the active conformation. Pogenberg, V., Guichou, J.F., Bourguet, W. Acta Crystallogr. D Biol. Crystallogr. (2004) [Pubmed]
  17. Inactivation of MED-1 elements in the TATA-less, initiator-less mouse thymidylate synthase promoter has no effect on promoter strength or the complex pattern of transcriptional start sites. Rudge, T.L., Johnson, L.F. J. Cell. Biochem. (1999) [Pubmed]
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