PMID- 9653119
OWN - NLM
STAT- MEDLINE
DCOM- 19980806
LR  - 20220420
IS  - 0027-8424 (Print)
IS  - 1091-6490 (Electronic)
IS  - 0027-8424 (Linking)
VI  - 95
IP  - 14
DP  - 1998 Jul 7
TI  - The TRAP220 component of a thyroid hormone receptor- associated protein (TRAP) 
      coactivator complex interacts directly with nuclear receptors in a 
      ligand-dependent fashion.
PG  - 7939-44
AB  - Cognate cDNAs are described for 2 of the 10 thyroid hormone receptor-associated 
      proteins (TRAPs) that are immunopurified with thyroid hormone receptor alpha 
      (TRalpha) from ligand-treated HeLa (alpha-2) cells. Both TRAP220 and TRAP100 
      contain LXXLL domains found in other nuclear receptor-interacting proteins and 
      both appear to reside in a single complex with other TRAPs (in the absence of 
      TR). However, only TRAP220 shows a direct ligand-dependent interaction with 
      TRalpha, and these interactions are mediated through the C terminus of TRalpha 
      and (at least in part) the LXXLL domains of TRAP220. TRAP220 also interacts with 
      other nuclear receptors [vitamin D receptor, retinoic acid receptor alpha, 
      retinoid X receptor alpha, peroxisome proliferation-activated receptor (PPAR) 
      alpha, PPARgamma and, to a lesser extent, estrogen receptor] in a 
      ligand-dependent manner, whereas TRAP100 shows only marginal interactions with 
      estrogen receptor, retinoid X receptor alpha, PPARalpha, and PPARgamma. 
      Consistent with these results, TRAP220 moderately stimulates human 
      TRalpha-mediated transcription in transfected cells, whereas a fragment 
      containing the LXXLL motifs acts as a dominant negative inhibitor of nuclear 
      receptor-mediated transcription both in transfected cells (TRalpha) and in cell 
      free transcription systems (TRalpha and vitamin D receptor). These studies 
      indicate that TRAP220 plays a major role in anchoring other TRAPs to TRalpha 
      during the function of the TRalpha-TRAP complex and, further, that TRAP220 
      (possibly along with other TRAPs) may be a global coactivator for the nuclear 
      receptor superfamily.
FAU - Yuan, C X
AU  - Yuan CX
AD  - Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, New 
      York, NY 10021, USA.
FAU - Ito, M
AU  - Ito M
FAU - Fondell, J D
AU  - Fondell JD
FAU - Fu, Z Y
AU  - Fu ZY
FAU - Roeder, R G
AU  - Roeder RG
LA  - eng
SI  - GENBANK/AF055994
SI  - GENBANK/AF055995
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (BRD8 protein, human)
RN  - 0 (Carrier Proteins)
RN  - 0 (Ligands)
RN  - 0 (MED1 protein, human)
RN  - 0 (Med1 protein, mouse)
RN  - 0 (Mediator Complex Subunit 1)
RN  - 0 (Receptors, Cytoplasmic and Nuclear)
RN  - 0 (Receptors, Thyroid Hormone)
RN  - 0 (Transcription Factors)
SB  - IM
EIN - Proc Natl Acad Sci U S A 1998 Nov 24;95(24):14584
MH  - 3T3 Cells
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites/genetics
MH  - Carrier Proteins/*chemistry/*genetics/*metabolism
MH  - Cloning, Molecular
MH  - Humans
MH  - Ligands
MH  - Mediator Complex Subunit 1
MH  - Mice
MH  - Molecular Sequence Data
MH  - Receptors, Cytoplasmic and Nuclear/*metabolism
MH  - *Receptors, Thyroid Hormone
MH  - *Transcription Factors
PMC - PMC20908
EDAT- 1998/07/08 00:00
MHDA- 1998/07/08 00:01
PMCR- 1999/01/07
CRDT- 1998/07/08 00:00
PHST- 1998/07/08 00:00 [pubmed]
PHST- 1998/07/08 00:01 [medline]
PHST- 1998/07/08 00:00 [entrez]
PHST- 1999/01/07 00:00 [pmc-release]
AID - 1618 [pii]
AID - 10.1073/pnas.95.14.7939 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1998 Jul 7;95(14):7939-44. doi: 
      10.1073/pnas.95.14.7939.