MED1

From Wikipedia, the free encyclopedia

Mediator complex subunit 1

Identifiers

MED1; PPARBP; PBP; CRSP1; CRSP200; DRIP205; DRIP230; MGC71488; PPARGBP; RB18A; TRAP220; TRIP2

External IDs

OMIM: 604311 MGI: 1100846 HomoloGene: 21002

Gene ontology
Molecular Function:	• DNA binding • chromatin binding • receptor activity • protein binding • ATP binding • RNA polymerase II transcription mediator activity • ligand-dependent nuclear receptor transcription coactivator activity • phosphopantetheine binding • vitamin D receptor binding • thyroid hormone receptor binding
Cellular Component:	• mediator complex • nucleus
Biological Process:	• in utero embryonic development • liver development • embryonic placenta development • DNA replication • transcription • regulation of transcription, DNA-dependent • transcription initiation from RNA polymerase II promoter • thyroid hormone generation • multicellular organismal development • brain development • androgen receptor signaling pathway • embryonic heart tube development • embryonic hindlimb morphogenesis • embryonic hemopoiesis • fat cell differentiation • positive regulation of transcription from RNA polymerase II promoter

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004774 (mRNA)
NP_004765 (protein)

NM_001080118 (mRNA)
NP_001073587 (protein)

Location

Chr 17: 34.82 - 34.86 Mb

Chr 11: 97.97 - 98.01 Mb

Pubmed search

[1]

[2]

Mediator complex subunit 1, also known as MED1, is a human gene.^[1]

The activation of gene transcription is a multistep process that is triggered by factors that recognize transcriptional enhancer sites in DNA. These factors work with co-activators to direct transcriptional initiation by the RNA polymerase II apparatus. The protein encoded by this gene is a subunit of the CRSP (cofactor required for SP1 activation) complex, which, along with TFIID, is required for efficient activation by SP1. This protein is also a component of other multisubunit complexes e.g. thyroid hormone receptor-(TR-) associated proteins which interact with TR and facilitate TR function on DNA templates in conjunction with initiation factors and cofactors. It also regulates p53-dependent apoptosis and it is essential for adipogenesis. This protein is known to have the ability to self-oligomerize.^[1]

[edit] References

^ ^a ^b Entrez Gene: PPARBP PPAR binding protein.

[edit] Further reading

Lee JW, Choi HS, Gyuris J, et al. (1995). "Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor.". Mol. Endocrinol. 9 (2): 243–54. PMID 7776974.
Fondell JD, Ge H, Roeder RG (1996). "Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex.". Proc. Natl. Acad. Sci. U.S.A. 93 (16): 8329–33. PMID 8710870.
Zhu Y, Qi C, Jain S, et al. (1997). "Isolation and characterization of PBP, a protein that interacts with peroxisome proliferator-activated receptor.". J. Biol. Chem. 272 (41): 25500–6. PMID 9325263.
Drané P, Barel M, Balbo M, Frade R (1998). "Identification of RB18A, a 205 kDa new p53 regulatory protein which shares antigenic and functional properties with p53.". Oncogene 15 (25): 3013–24. doi:10.1038/sj.onc.1201492. PMID 9444950.
Yuan CX, Ito M, Fondell JD, et al. (1998). "The TRAP220 component of a thyroid hormone receptor- associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion.". Proc. Natl. Acad. Sci. U.S.A. 95 (14): 7939–44. PMID 9653119.
Ryu S, Zhou S, Ladurner AG, Tjian R (1999). "The transcriptional cofactor complex CRSP is required for activity of the enhancer-binding protein Sp1.". Nature 397 (6718): 446–50. doi:10.1038/17141. PMID 9989412.
Gu W, Malik S, Ito M, et al. (1999). "A novel human SRB/MED-containing cofactor complex, SMCC, involved in transcription regulation.". Mol. Cell 3 (1): 97–108. PMID 10024883.
Ito M, Yuan CX, Malik S, et al. (1999). "Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators.". Mol. Cell 3 (3): 361–70. PMID 10198638.
Rachez C, Lemon BD, Suldan Z, et al. (1999). "Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex.". Nature 398 (6730): 824–8. doi:10.1038/19783. PMID 10235266.
Näär AM, Beaurang PA, Zhou S, et al. (1999). "Composite co-activator ARC mediates chromatin-directed transcriptional activation.". Nature 398 (6730): 828–32. doi:10.1038/19789. PMID 10235267.
Atkins GB, Hu X, Guenther MG, et al. (1999). "Coactivators for the orphan nuclear receptor RORalpha.". Mol. Endocrinol. 13 (9): 1550–7. PMID 10478845.
Zhu Y, Qi C, Jain S, et al. (1999). "Amplification and overexpression of peroxisome proliferator-activated receptor binding protein (PBP/PPARBP) gene in breast cancer.". Proc. Natl. Acad. Sci. U.S.A. 96 (19): 10848–53. PMID 10485914.
Rachez C, Gamble M, Chang CP, et al. (2000). "The DRIP complex and SRC-1/p160 coactivators share similar nuclear receptor binding determinants but constitute functionally distinct complexes.". Mol. Cell. Biol. 20 (8): 2718–26. PMID 10733574.
Frade R, Balbo M, Barel M (2001). "RB18A, whose gene is localized on chromosome 17q12-q21.1, regulates in vivo p53 transactivating activity.". Cancer Res. 60 (23): 6585–9. PMID 11118038.
Zilliacus J, Holter E, Wakui H, et al. (2001). "Regulation of glucocorticoid receptor activity by 14--3-3-dependent intracellular relocalization of the corepressor RIP140.". Mol. Endocrinol. 15 (4): 501–11. PMID 11266503.
Crawford SE, Qi C, Misra P, et al. (2002). "Defects of the heart, eye, and megakaryocytes in peroxisome proliferator activator receptor-binding protein (PBP) null embryos implicate GATA family of transcription factors.". J. Biol. Chem. 277 (5): 3585–92. doi:10.1074/jbc.M107995200. PMID 11724781.
Frade R, Balbo M, Barel M (2002). "RB18A regulates p53-dependent apoptosis.". Oncogene 21 (6): 861–6. doi:10.1038/sj.onc.1205177. PMID 11840331.
Kang YK, Guermah M, Yuan CX, Roeder RG (2002). "The TRAP/Mediator coactivator complex interacts directly with estrogen receptors alpha and beta through the TRAP220 subunit and directly enhances estrogen receptor function in vitro.". Proc. Natl. Acad. Sci. U.S.A. 99 (5): 2642–7. doi:10.1073/pnas.261715899. PMID 11867769.
Misra P, Qi C, Yu S, et al. (2002). "Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation.". J. Biol. Chem. 277 (22): 20011–9. doi:10.1074/jbc.M201739200. PMID 11912212.
Ge K, Guermah M, Yuan CX, et al. (2002). "Transcription coactivator TRAP220 is required for PPAR gamma 2-stimulated adipogenesis.". Nature 417 (6888): 563–7. doi:10.1038/417563a. PMID 12037571.