PMID- 10406464
OWN - NLM
STAT- MEDLINE
DCOM- 19990921
LR  - 20091119
IS  - 0888-8809 (Print)
IS  - 0888-8809 (Linking)
VI  - 13
IP  - 7
DP  - 1999 Jul
TI  - Identification of mouse TRAP100: a transcriptional coregulatory factor for
      thyroid hormone and vitamin D receptors.
PG  - 1130-40
AB  - Nuclear hormone receptors (NRs) regulate transcription in part by recruiting
      distinct transcriptional coregulatory complexes to target gene promoters. The
      thyroid hormone receptor (TR) was recently purified from thyroid hormone-cultured
      HeLa cells in association with a complex of novel nuclear proteins termed TRAPs
      (thyroid hormone receptor-associated proteins) ranging in size from 20 to 240
      kDa. The TRAP complex markedly enhances TR-mediated transcription in vitro,
      suggesting a coactivator role for one or more of the TRAP components. Here we
      present the mouse cDNA for the 100-kDa component of the TRAP complex (mTRAP100). 
      The mTRAP100 protein contains seven LxxLL motifs thought to be potential binding 
      surfaces for liganded NRs, yet surprisingly fails to interact with TR and other
      NRs in vitro. By contrast, mTRAP100 coprecipitates in vivo with another component
      of the TRAP complex (TRAP220), which directly contacts TR and the vitamin D
      receptor in a ligand-dependent manner. Our findings thus suggest that TRAP100 is 
      targeted to NRs in association with TRAP complexes specifically containing
      TRAP220. Transient overexpression of mTRAP100 in mammalian cells further enhances
      ligand-dependent transcription by both TR and the vitamin D receptor, revealing a
      functional role for mTRAP100 in NR-mediated transactivation. The presence of an
      intrinsic mTRAP100 transactivation function is suggested by the ability of
      mTRAP100 to activate transcription constitutively when tethered to the GAL4
      DNA-binding domain. Collectively, these findings suggest that TRAP100, in concert
      with other TRAPs, plays an important functional role in mediating transactivation
      by specific NRs.
FAU - Zhang, J
AU  - Zhang J
AD  - Department of Physiology, University of Maryland School of Medicine, Baltimore
      21201, USA.
FAU - Fondell, J D
AU  - Fondell JD
LA  - eng
SI  - GENBANK/AF126543
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Mol Endocrinol
JT  - Molecular endocrinology (Baltimore, Md.)
JID - 8801431
RN  - 0 (Carrier Proteins)
RN  - 0 (DNA, Complementary)
RN  - 0 (MED1 protein, human)
RN  - 0 (MED24 protein, human)
RN  - 0 (Med1 protein, mouse)
RN  - 0 (Med24 protein, mouse)
RN  - 0 (Mediator Complex)
RN  - 0 (Mediator Complex Subunit 1)
RN  - 0 (Receptors, Calcitriol)
RN  - 0 (Receptors, Cytoplasmic and Nuclear)
RN  - 0 (Receptors, Thyroid Hormone)
RN  - 0 (Transcription Factors)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Carrier Proteins/metabolism
MH  - Cells, Cultured
MH  - Chemical Precipitation
MH  - DNA, Complementary
MH  - Humans
MH  - Mediator Complex
MH  - Mediator Complex Subunit 1
MH  - Mice
MH  - Molecular Sequence Data
MH  - Receptors, Calcitriol/genetics/*metabolism
MH  - Receptors, Cytoplasmic and Nuclear/metabolism
MH  - Receptors, Thyroid Hormone/genetics/*metabolism
MH  - Sequence Homology, Amino Acid
MH  - Transcription Factors/*genetics/*metabolism
MH  - Transcription, Genetic
MH  - Transcriptional Activation
EDAT- 1999/07/16 00:00
MHDA- 1999/07/16 00:01
CRDT- 1999/07/16 00:00
PHST- 1999/07/16 00:00 [pubmed]
PHST- 1999/07/16 00:01 [medline]
PHST- 1999/07/16 00:00 [entrez]
AID - 10.1210/mend.13.7.0295 [doi]
PST - ppublish
SO  - Mol Endocrinol. 1999 Jul;13(7):1130-40. doi: 10.1210/mend.13.7.0295.