PMID- 7916146
OWN - NLM
STAT- MEDLINE
DCOM- 19941013
LR  - 20131121
IS  - 0950-9232 (Print)
IS  - 0950-9232 (Linking)
VI  - 9
IP  - 10
DP  - 1994 Oct
TI  - c-ErbA, but not v-ErbA, competes with a putative erythroid repressor for binding 
      to the carbonic anhydrase II promoter.
PG  - 2853-67
AB  - The carbonic anhydrase II (CAII) gene is the only known gene identified as direct 
      target for v-ErbA-mediated repression in avian erythroleukemic cells transformed 
      by Avian Erythroblastosis Virus (AEV). This gene is transcriptionally activated 
      by thyroid hormone (T3) in normal erythrocytic cells. In this work we have 
      analysed the molecular basis of the transcriptional control of the CAII gene by 
      c-ErbA and v-ErbA. We show that several domains in the promoter control hormonal 
      regulation of transcription. One domain proximal to the TATA box mediates T3 
      response but contains no identified binding site for c-ErbA. An other domain 
      termed PAL2 is approximately 600 bp upstream the transcription initiation site 
      and contains a c-ErbA binding site. We show that when it is associated to a 
      heterologous promoter this site mediates transcriptional repression in 
      erythrocytic cells but not in HeLa cells. Moreover, this site binds a nuclear 
      erythrocyte-specific factor that we called NFX, which is different from c-ErbA. 
      heterodimers between c-ErbA and the 9-cis retinoic acid receptor (RXR) compete 
      with NFX for binding to PAL2. In contrast, v-ErbA alone or in association with 
      RXR is a very poor competitor and is unable to chase NFX out of the PAL2 site. We 
      propose that NFX is a transcription repressor whose activity is inhibited by 
      c-ErbA but not v-ErbA. This mechanism might contribute to the overall regulation 
      of the carbonic anhydrase II promoter. These data illustrate another possible 
      mechanism through which v-ErbA might antagonize the function of c-ErbA in 
      controlling gene expression.
FAU - Rascle, A
AU  - Rascle A
AD  - Laboratoire de Biologie Moleculaire et Cellulaire, CNRS UMR49, INRA, Ecole 
      Normale Superieure de Lyon, France.
FAU - Ghysdael, J
AU  - Ghysdael J
FAU - Samarut, J
AU  - Samarut J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Oncogene
JT  - Oncogene
JID - 8711562
RN  - 0 (Nuclear Proteins)
RN  - 0 (Oligodeoxyribonucleotides)
RN  - 0 (Oncogene Proteins v-erbA)
RN  - 0 (Receptors, Retinoic Acid)
RN  - 0 (Receptors, Thyroid Hormone)
RN  - 0 (Repressor Proteins)
RN  - 0 (Retroviridae Proteins, Oncogenic)
RN  - 06LU7C9H1V (Triiodothyronine)
RN  - 5688UTC01R (Tretinoin)
RN  - EC 4.2.1.1 (Carbonic Anhydrases)
SB  - IM
GS  - CAII
MH  - Animals
MH  - Base Sequence
MH  - Binding, Competitive
MH  - Carbonic Anhydrases/*genetics
MH  - Chick Embryo
MH  - Erythrocytes/*metabolism
MH  - HeLa Cells
MH  - Humans
MH  - Molecular Sequence Data
MH  - Nuclear Proteins/metabolism
MH  - Oligodeoxyribonucleotides
MH  - Oncogene Proteins v-erbA
MH  - Osmosis
MH  - *Promoter Regions, Genetic
MH  - Receptors, Retinoic Acid/metabolism
MH  - Receptors, Thyroid Hormone/*metabolism
MH  - Repressor Proteins/*metabolism
MH  - Retroviridae Proteins, Oncogenic/*metabolism
MH  - Transcription, Genetic
MH  - Transcriptional Activation
MH  - Transfection
MH  - Tretinoin/pharmacology
MH  - Triiodothyronine/pharmacology
MH  - Tumor Cells, Cultured
EDAT- 1994/10/01 00:00
MHDA- 1994/10/01 00:01
CRDT- 1994/10/01 00:00
PHST- 1994/10/01 00:00 [pubmed]
PHST- 1994/10/01 00:01 [medline]
PHST- 1994/10/01 00:00 [entrez]
PST - ppublish
SO  - Oncogene. 1994 Oct;9(10):2853-67.