PMID- 10593900
OWN - NLM
STAT- MEDLINE
DCOM- 20000127
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 51
DP  - 1999 Dec 17
TI  - MRG1 binds to the LIM domain of Lhx2 and may function as a coactivator to
      stimulate glycoprotein hormone alpha-subunit gene expression.
PG  - 36159-67
AB  - Tissue-specific expression of the alpha-subunit gene of glycoprotein hormones
      involves an enhancer element designated the pituitary glycoprotein basal element,
      which interacts with the LIM homeodomain transcription factor, Lhx2. In the
      present studies we have explored the function of the LIM domain of Lhx2 in
      stimulating alpha-subunit transcription. When fused to the GAL4 DNA-binding
      domain, the LIM domain of Lhx2 was shown to contain a transcriptional activation 
      domain. Furthermore, in the context of an alpha-subunit reporter gene in which a 
      GAL4-binding site replaced the pituitary glycoprotein basal element, the LIM
      domain enhanced both basal and Ras-mediated transcription. In addition, a
      synergistic response to Ras activation was observed when the Lhx2 LIM domain and 
      the transactivation domain of Elk1 are directed to a minimal reporter gene. A
      yeast two-hybrid screen identified the recently described melanocyte-specific
      gene-related gene 1 (MRG1) as an Lhx2 LIM-interacting protein. MRG1 was shown to 
      bind Lhx2 in vitro, and a co-immunoprecipitation assay provided evidence that
      endogenous MRG1 forms a complex with Lhx2 in alphaT3-1 cells. Expression of MRG1 
      in alphaT3-1 cells enhanced alpha-subunit reporter gene activity. MRG1 was also
      shown to bind in vitro to the TATA-binding protein and the transcriptional
      coactivator, p300. These data suggest a model in which the Lhx2 LIM domain
      activates transcription through interaction with MRG1 leading to recruitment of
      p300/CBP and the TATA-binding protein.
FAU - Glenn, D J
AU  - Glenn DJ
AD  - Department of Cell and Developmental Biology, Oregon Health Sciences University, 
      Portland, Oregon 97201, USA.
FAU - Maurer, R A
AU  - Maurer RA
LA  - eng
GR  - DK36407/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Cited2 protein, mouse)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Glycoproteins)
RN  - 0 (Homeodomain Proteins)
RN  - 0 (Hormones)
RN  - 0 (LIM-Homeodomain Proteins)
RN  - 0 (Lhx2 protein, mouse)
RN  - 0 (Repressor Proteins)
RN  - 0 (Trans-Activators)
RN  - 0 (Transcription Factors)
SB  - IM
MH  - Animals
MH  - Binding Sites
MH  - Cell Line
MH  - DNA-Binding Proteins/chemistry/metabolism
MH  - Gene Expression Regulation
MH  - Glycoproteins/chemistry/genetics/*metabolism
MH  - Homeodomain Proteins/chemistry/*metabolism
MH  - Hormones/chemistry/genetics/metabolism
MH  - LIM-Homeodomain Proteins
MH  - Protein Binding
MH  - *Repressor Proteins
MH  - Trans-Activators/chemistry/*metabolism
MH  - Transcription Factors/chemistry/*metabolism
EDAT- 1999/12/14 00:00
MHDA- 1999/12/14 00:01
CRDT- 1999/12/14 00:00
PHST- 1999/12/14 00:00 [pubmed]
PHST- 1999/12/14 00:01 [medline]
PHST- 1999/12/14 00:00 [entrez]
AID - 10.1074/jbc.274.51.36159 [doi]
AID - S0021-9258(19)53144-1 [pii]
PST - ppublish
SO  - J Biol Chem. 1999 Dec 17;274(51):36159-67. doi: 10.1074/jbc.274.51.36159.