PMID- 10673374
OWN - NLM
STAT- MEDLINE
DCOM- 20000309
LR  - 20131121
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 267
IP  - 3
DP  - 2000 Jan 27
TI  - Biochemical evidence for a 170-kilodalton, AF-2-dependent vitamin D 
      receptor/retinoid X receptor coactivator that is highly expressed in osteoblasts.
PG  - 813-9
AB  - Human vitamin D receptor (hVDR) fused to glutathione S-transferase was utilized 
      to detect a VDR-interacting protein (VIP) of approximately 170 kDa. VIP(170) is 
      expressed in osteoblast-like ROS 17/2.8 cells and, to a lesser extent, in COS-7 
      and HeLa cells. VIP(170) may be a coactivator because it interacts only with 
      1,25-dihydroxyvitamin D(3) (1,25(OH)(2)D(3)) ligand-bound hVDR and because a 
      mutation (E420A) in the activation function-2 (AF-2) of hVDR abolishes both 
      receptor-mediated transactivation and VIP(170) binding. Unlike L254G hVDR, a 
      heterodimerization mutant with an intact AF-2, the E420A mutant is only partially 
      attenuated in its association with the retinoid X receptor (RXR) DNA-binding 
      partner. Finally, the ability of overexpressed hVDR to squelch glucocorticoid 
      receptor-mediated transactivation is lost in both the L254G and E420A mutants. 
      These results suggest that several protein-protein interactions, including VDR 
      association with RXR and VIP(170), are required for stabilization of a multimeric 
      complex that transduces the signal for 1,25(OH)(2)D(3)-elicited transactivation.
CI  - Copyright 2000 Academic Press.
FAU - Jurutka, P W
AU  - Jurutka PW
AD  - Department of Biochemistry, College of Medicine, University of Arizona, Tucson, 
      Arizona, 85724, USA.
FAU - Remus, L S
AU  - Remus LS
FAU - Whitfield, G K
AU  - Whitfield GK
FAU - Galligan, M A
AU  - Galligan MA
FAU - Haussler, C A
AU  - Haussler CA
FAU - Haussler, M R
AU  - Haussler MR
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (DRIP, VDR interacting protein complex)
RN  - 0 (MED4 protein, human)
RN  - 0 (Mediator Complex)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Receptors, Retinoic Acid)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Retinoid X Receptors)
RN  - 0 (Trans-Activators)
RN  - 0 (Transcription Factors)
RN  - 7S5I7G3JQL (Dexamethasone)
RN  - FXC9231JVH (Calcitriol)
SB  - IM
MH  - Amino Acid Substitution
MH  - Animals
MH  - COS Cells
MH  - Calcitriol/pharmacology
MH  - Dexamethasone/pharmacology
MH  - Dimerization
MH  - HeLa Cells
MH  - Humans
MH  - Mediator Complex
MH  - Molecular Weight
MH  - Mutagenesis, Site-Directed
MH  - Nuclear Proteins/biosynthesis/genetics/*metabolism
MH  - Osteoblasts/*metabolism
MH  - Osteosarcoma
MH  - Receptors, Retinoic Acid/*metabolism
MH  - Recombinant Fusion Proteins/biosynthesis
MH  - Retinoid X Receptors
MH  - *Trans-Activators
MH  - Transcription Factors/*metabolism
MH  - Transcription, Genetic/drug effects
MH  - Transcriptional Activation/drug effects
MH  - Tumor Cells, Cultured
EDAT- 2000/02/16 09:00
MHDA- 2000/03/11 09:00
CRDT- 2000/02/16 09:00
PHST- 2000/02/16 09:00 [pubmed]
PHST- 2000/03/11 09:00 [medline]
PHST- 2000/02/16 09:00 [entrez]
AID - S0006-291X(99)92044-2 [pii]
AID - 10.1006/bbrc.1999.2044 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 2000 Jan 27;267(3):813-9. doi: 
      10.1006/bbrc.1999.2044.