PMID- 16357047
OWN - NLM
STAT- MEDLINE
DCOM- 20060413
LR  - 20191210
IS  - 0013-7227 (Print)
IS  - 0013-7227 (Linking)
VI  - 147
IP  - 3
DP  - 2006 Mar
TI  - The interaction of TRbeta1-N terminus with steroid receptor coactivator-1 (SRC-1) 
      serves a full transcriptional activation function of SRC-1.
PG  - 1452-7
AB  - Steroid receptor coactivator-1 (SRC-1) plays a crucial role in nuclear 
      receptor-mediated transcription including thyroid hormone receptor (TR)-dependent 
      gene expression. Interaction of the TR-ligand binding domain and SRC-1 through 
      LXXLL motifs is required for this action. However, potential interactions between 
      the TRbeta1-N terminus (N) and SRC-1 have not been explored and thus are examined 
      in this manuscript. Far-Western studies showed that protein construct containing 
      TRbeta1-N + DNA binding domain (DBD) bound to nuclear receptor binding domain 
      (NBD)-1 (amino acid residue, aa 595-780) of SRC-1 without ligand. Mammalian 
      two-hybrid studies showed that NBD-1, as well as SRC-1 (aa 595-1440), bound to 
      TRbeta1-N+DBD in the absence of ligand in CV-1 cells. However, NBD-2 (aa 
      1237-1440) did not bind to this protein. Glutathione-S-transferase pull-down 
      studies showed that TRbeta1-N (aa 1-105) bound to the broad region of SRC-1-C 
      terminus. Expression vectors encoding a series of truncations and/or point 
      mutations of TRbeta1 were used in transient transfection-based reporter assays in 
      CV-1 cells. N-terminal truncated TRbeta1 (DeltaN-TRbeta1) showed lower activity 
      than that of wild-type in both artificial F2-thyroid hormone response element and 
      native malic enzyme response element. These results suggest that there is the 
      interaction between N terminus of TRbeta1 and SRC-1, which may serve a full 
      activation of SRC-1, together with activation function-2 on TRbeta1-mediated 
      transcription.
FAU - Iwasaki, Toshiharu
AU  - Iwasaki T
AD  - Department of Integrative Physiology, Gunma University Graduate School of 
      Medicine, 3-39-22 Showa-machi, Maebashi 371-8511, Gunma, Japan. 
      tiwasaki@med.gunma-u.ac.jp
FAU - Takeshita, Akira
AU  - Takeshita A
FAU - Miyazaki, Wataru
AU  - Miyazaki W
FAU - Chin, William W
AU  - Chin WW
FAU - Koibuchi, Noriyuki
AU  - Koibuchi N
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20051215
PL  - United States
TA  - Endocrinology
JT  - Endocrinology
JID - 0375040
RN  - 0 (DNA, Complementary)
RN  - 0 (Ligands)
RN  - 0 (Receptors, Thyroid Hormone)
RN  - 0 (Transcription Factors)
RN  - EC 2.3.1.48 (Histone Acetyltransferases)
RN  - EC 2.3.1.48 (Nuclear Receptor Coactivator 1)
RN  - EC 2.5.1.18 (Glutathione Transferase)
SB  - IM
MH  - Animals
MH  - Blotting, Western
MH  - Cell Line
MH  - Chlorocebus aethiops
MH  - DNA, Complementary/metabolism
MH  - Genetic Vectors
MH  - Glutathione Transferase/metabolism
MH  - Histone Acetyltransferases
MH  - Ligands
MH  - Nuclear Receptor Coactivator 1
MH  - Plasmids/metabolism
MH  - Point Mutation
MH  - Protein Binding
MH  - Protein Structure, Tertiary
MH  - Receptors, Thyroid Hormone/metabolism
MH  - Response Elements
MH  - Transcription Factors/metabolism/*physiology
MH  - Transcription, Genetic
MH  - *Transcriptional Activation
MH  - Transfection
EDAT- 2005/12/17 09:00
MHDA- 2006/04/14 09:00
CRDT- 2005/12/17 09:00
PHST- 2005/12/17 09:00 [pubmed]
PHST- 2006/04/14 09:00 [medline]
PHST- 2005/12/17 09:00 [entrez]
AID - en.2005-0782 [pii]
AID - 10.1210/en.2005-0782 [doi]
PST - ppublish
SO  - Endocrinology. 2006 Mar;147(3):1452-7. doi: 10.1210/en.2005-0782. Epub 2005 Dec 
      15.