PMID- 10409727
OWN - NLM
STAT- MEDLINE
DCOM- 19990819
LR  - 20190508
IS  - 0270-7306 (Print)
IS  - 0270-7306 (Linking)
VI  - 19
IP  - 8
DP  - 1999 Aug
TI  - Purification and identification of p68 RNA helicase acting as a transcriptional
      coactivator specific for the activation function 1 of human estrogen receptor
      alpha.
PG  - 5363-72
AB  - The estrogen receptor (ER) regulates the expression of target genes in a
      ligand-dependent manner. The ligand-dependent activation function AF-2 of the ER 
      is located in the ligand binding domain (LBD), while the N-terminal A/B domain
      (AF-1) functions in a ligand-independent manner when isolated from the LBD. AF-1 
      and AF-2 exhibit cell type and promoter context specificity. Furthermore, the
      AF-1 activity of the human ERalpha (hERalpha) is enhanced through phosphorylation
      of the Ser(118) residue by mitogen-activated protein kinase (MAPK). From MCF-7
      cells, we purified and cloned a 68-kDa protein (p68) which interacted with the
      A/B domain but not with the LBD of hERalpha. Phosphorylation of hERalpha Ser(118)
      potentiated the interaction with p68. We demonstrate that p68 enhanced the
      activity of AF-1 but not AF-2 and the estrogen-induced as well as the
      anti-estrogen-induced transcriptional activity of the full-length ERalpha in a
      cell-type-specific manner. However, it did not potentiate AF-1 or AF-2 of ERbeta,
      androgen receptor, retinoic acid receptor alpha, or mineralocorticoid receptor.
      We also show that the RNA helicase activity previously ascribed to p68 is
      dispensable for the ERalpha AF-1 coactivator activity and that p68 binds to CBP
      in vitro. Furthermore, the interaction region for p68 in the ERalpha A/B domain
      was essential for the full activity of hERalpha AF-1. Taken together, these
      findings show that p68 acts as a coactivator specific for the ERalpha AF-1 and
      strongly suggest that the interaction between p68 and the hERalpha A/B domain is 
      regulated by MAPK-induced phosphorylation of Ser(118).
FAU - Endoh, H
AU  - Endoh H
AD  - Molecular Medicine Laboratories, Institute for Drug Discovery Research,
      Yamanouchi Pharmaceutical, Tsukuba, Ibaraki 305-8585, Japan.
FAU - Maruyama, K
AU  - Maruyama K
FAU - Masuhiro, Y
AU  - Masuhiro Y
FAU - Kobayashi, Y
AU  - Kobayashi Y
FAU - Goto, M
AU  - Goto M
FAU - Tai, H
AU  - Tai H
FAU - Yanagisawa, J
AU  - Yanagisawa J
FAU - Metzger, D
AU  - Metzger D
FAU - Hashimoto, S
AU  - Hashimoto S
FAU - Kato, S
AU  - Kato S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Retracted Publication
PL  - United States
TA  - Mol Cell Biol
JT  - Molecular and cellular biology
JID - 8109087
RN  - 0 (Estrogen Receptor alpha)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Receptors, Estrogen)
RN  - 0 (Recombinant Fusion Proteins)
RN  - EC 2.7.- (Protein Kinases)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinases)
RN  - EC 3.6.1.- (Ddx5 protein, human)
RN  - EC 3.6.4.13 (DEAD-box RNA Helicases)
RN  - EC 3.6.4.13 (RNA Helicases)
SB  - IM
RIN - Mol Cell Biol. 2014 Mar;34(5):915. PMID: 24509260
MH  - Adenocarcinoma/pathology
MH  - Amino Acid Sequence
MH  - Animals
MH  - Breast Neoplasms/pathology
MH  - Calcium-Calmodulin-Dependent Protein Kinases/physiology
MH  - DEAD-box RNA Helicases
MH  - Estrogen Receptor alpha
MH  - Female
MH  - *Gene Expression Regulation
MH  - Humans
MH  - Molecular Sequence Data
MH  - Neoplasm Proteins/isolation & purification/physiology
MH  - Phosphorylation
MH  - Protein Binding
MH  - *Protein Kinases
MH  - Protein Processing, Post-Translational
MH  - *Protein Structure, Tertiary
MH  - RNA Helicases/*isolation & purification/physiology
MH  - Rabbits
MH  - Receptors, Estrogen/chemistry/*physiology
MH  - Recombinant Fusion Proteins/physiology
MH  - Sequence Analysis
MH  - *Transcription, Genetic
MH  - Tumor Cells, Cultured
PMC - PMC84379
EDAT- 1999/07/20 00:00
MHDA- 1999/07/20 00:01
CRDT- 1999/07/20 00:00
PHST- 1999/07/20 00:00 [pubmed]
PHST- 1999/07/20 00:01 [medline]
PHST- 1999/07/20 00:00 [entrez]
AID - 10.1128/mcb.19.8.5363 [doi]
PST - ppublish
SO  - Mol Cell Biol. 1999 Aug;19(8):5363-72. doi: 10.1128/mcb.19.8.5363.