PMID- 10235266
OWN - NLM
STAT- MEDLINE
DCOM- 19990614
LR  - 20091119
IS  - 0028-0836 (Print)
IS  - 0028-0836 (Linking)
VI  - 398
IP  - 6730
DP  - 1999 Apr 29
TI  - Ligand-dependent transcription activation by nuclear receptors requires the DRIP 
      complex.
PG  - 824-8
AB  - Nuclear receptors modulate the transcription of genes in direct response to small
      lipophilic ligands. Binding to ligands induces conformational changes in the
      nuclear receptors that enable the receptors to interact with several types of
      cofactor that are critical for transcription activation (transactivation). We
      previously described a distinct set of ligand-dependent proteins called DRIPs,
      which interact with the vitamin D receptor (VDR); together, these proteins
      constitute a new cofactor complex. DRIPs bind to several nuclear receptors and
      mediate ligand-dependent enhancement of transcription by VDR and the
      thyroid-hormone receptor in cell-free transcription assays. Here we report the
      identities of thirteen DRIPs that constitute this complex, and show that the
      complex has a central function in hormone-dependent transactivation by VDR on
      chromatin templates. The DRIPs are almost indistinguishable from components of
      another new cofactor complex called ARC, which is recruited by other types of
      transcription activators to mediate transactivation on chromatin-assembled
      templates. Several DRIP/ARC subunits are also components of other potentially
      related cofactors, such as CRSP, NAT, SMCC and the mouse Mediator, indicating
      that unique classes of activators may share common sets or subsets of cofactors. 
      The role of nuclear-receptor ligands may, in part, be to recruit such a cofactor 
      complex to the receptor and, in doing so, to enhance transcription of target
      genes.
FAU - Rachez, C
AU  - Rachez C
AD  - Cell Biology Program, Memorial Sloan-Kettering Cancer Center, Graduate School of 
      Medical Sciences, Cornell University, New York, New York 10021, USA.
FAU - Lemon, B D
AU  - Lemon BD
FAU - Suldan, Z
AU  - Suldan Z
FAU - Bromleigh, V
AU  - Bromleigh V
FAU - Gamble, M
AU  - Gamble M
FAU - Naar, A M
AU  - Naar AM
FAU - Erdjument-Bromage, H
AU  - Erdjument-Bromage H
FAU - Tempst, P
AU  - Tempst P
FAU - Freedman, L P
AU  - Freedman LP
LA  - eng
SI  - GENBANK/AF105332
SI  - GENBANK/AF105421
SI  - GENBANK/AF106934
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Nature
JT  - Nature
JID - 0410462
RN  - 0 (CRSP protein, human)
RN  - 0 (Carrier Proteins)
RN  - 0 (Chromatin)
RN  - 0 (DRIP, VDR interacting protein complex)
RN  - 0 (Ligands)
RN  - 0 (MED1 protein, human)
RN  - 0 (MED14 protein, human)
RN  - 0 (MED23 protein, human)
RN  - 0 (MED4 protein, human)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Med1 protein, mouse)
RN  - 0 (Med17 protein, human)
RN  - 0 (Mediator Complex)
RN  - 0 (Mediator Complex Subunit 1)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Receptors, Calcitriol)
RN  - 0 (Trans-Activators)
RN  - 0 (Transcription Factors)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Carrier Proteins/physiology
MH  - Chromatin/physiology
MH  - Cloning, Molecular
MH  - Drosophila
MH  - HeLa Cells
MH  - Humans
MH  - Ligands
MH  - Macromolecular Substances
MH  - Mediator Complex
MH  - Mediator Complex Subunit 1
MH  - Mice
MH  - Molecular Sequence Data
MH  - Nuclear Proteins/chemistry/*physiology
MH  - Receptors, Calcitriol/*physiology
MH  - Sequence Homology, Amino Acid
MH  - *Trans-Activators
MH  - *Transcription Factors
MH  - *Transcriptional Activation
EDAT- 1999/05/11 02:03
MHDA- 2001/03/23 10:01
CRDT- 1999/05/11 02:03
PHST- 1999/05/11 02:03 [pubmed]
PHST- 2001/03/23 10:01 [medline]
PHST- 1999/05/11 02:03 [entrez]
AID - 10.1038/19783 [doi]
PST - ppublish
SO  - Nature. 1999 Apr 29;398(6730):824-8. doi: 10.1038/19783.