PMID- 15698540
OWN - NLM
STAT- MEDLINE
DCOM- 20050408
LR  - 20191210
IS  - 0960-0760 (Print)
IS  - 0960-0760 (Linking)
VI  - 92
IP  - 5
DP  - 2004 Dec
TI  - FLASH interacts with p160 coactivator subtypes and differentially suppresses 
      transcriptional activity of steroid hormone receptors.
PG  - 357-63
AB  - We previously reported that tumor necrosis factor alpha receptor- and 
      Fas-associated FLASH interacts with one of the p160 nuclear receptor 
      coactivators, glucocorticoid receptor-interacting protein (GRIP) 1, at its 
      nuclear receptor-binding (NRB) domain, and that inhibits the transcriptional 
      activity of the glucocorticoid receptor (GR) by interfering with association of 
      GR and GRIP1. Here, we further examined the specificity of FLASH suppressive 
      effect and the physical/functional interactions between this protein and two 
      other p160 family subtypes. The suppressive effect of FLASH on GR transactivation 
      was observed in several cell lines and on the chromatin-integrated mouse mammary 
      tumor virus (MMTV) promoter. FLASH strongly interacted with the NRB domain of the 
      thyroid hormone receptor activator molecule (TRAM) 1, a member of the steroid 
      hormone receptor coactivator (SRC) 3/nuclear receptor coactivator (N-CoA) 3 
      subtypes, as well as with SRC2/N-CoA2 p160 coactivator GRIP1, while its 
      interaction with SRC1a, one of the SRC1/N-CoA1 proteins, was faint in yeast 
      two-hybrid assays. Accordingly, FLASH strongly suppressed TRAM1- and 
      GRIP1-induced enhancement of GR-stimulated transactivation of the MMTV promoter 
      in HCT116 cells, while it did not affect SRC1a-induced potentiation of 
      transcription. Furthermore, FLASH suppressed androgen- and progesterone 
      receptor-induced transcriptional activity, but did not influence estrogen 
      receptor-induced transactivation, possibly due to their preferential use of p160 
      coactivators in HCT116 and HeLa cells. Thus, FLASH differentially suppresses 
      steroid hormone receptor-induced transcriptional activity by interfering with 
      their association with SRC2/N-CoA2 and SRC3/N-CoA3 but not with SRC1/N-CoA1.
FAU - Kino, Tomoshige
AU  - Kino T
AD  - Pediatric and Reproductive Endocrinology Branch, National Institute of Child 
      Health and Human Development, Building 10, Clinical Research Center, Room 1-3140 
      , 10 Center Drive, MSC 1109, Bethesda, MD 20892-1109, USA. kinot@mail.nih.gov
FAU - Ichijo, Takamasa
AU  - Ichijo T
FAU - Chrousos, George P
AU  - Chrousos GP
LA  - eng
PT  - Journal Article
DEP - 20041219
PL  - England
TA  - J Steroid Biochem Mol Biol
JT  - The Journal of steroid biochemistry and molecular biology
JID - 9015483
RN  - 0 (Apoptosis Regulatory Proteins)
RN  - 0 (CASP8AP2 protein, human)
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (NCOA2 protein, human)
RN  - 0 (Nuclear Receptor Coactivator 2)
RN  - 0 (Receptors, Steroid)
RN  - 0 (Transcription Factors)
SB  - IM
MH  - Animals
MH  - Apoptosis Regulatory Proteins
MH  - Calcium-Binding Proteins/genetics/*metabolism
MH  - Cell Line
MH  - Chlorocebus aethiops
MH  - Humans
MH  - Nuclear Receptor Coactivator 2
MH  - Protein Binding
MH  - Receptors, Steroid/*antagonists & inhibitors/genetics/*metabolism
MH  - Transcription Factors/*classification/*metabolism
MH  - Transcription, Genetic/*genetics
MH  - Transcriptional Activation/genetics
EDAT- 2005/02/09 09:00
MHDA- 2005/04/09 09:00
CRDT- 2005/02/09 09:00
PHST- 2003/10/08 00:00 [received]
PHST- 2004/09/09 00:00 [accepted]
PHST- 2005/02/09 09:00 [pubmed]
PHST- 2005/04/09 09:00 [medline]
PHST- 2005/02/09 09:00 [entrez]
AID - S0960-0760(04)00374-7 [pii]
AID - 10.1016/j.jsbmb.2004.09.003 [doi]
PST - ppublish
SO  - J Steroid Biochem Mol Biol. 2004 Dec;92(5):357-63. doi: 
      10.1016/j.jsbmb.2004.09.003. Epub 2004 Dec 19.