PMID- 11316810
OWN - NLM
STAT- MEDLINE
DCOM- 20010809
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 276
IP  - 27
DP  - 2001 Jul 6
TI  - The reciprocal role of Egr-1 and Sp family proteins in regulation of the PTP1B 
      promoter in response to the p210 Bcr-Abl oncoprotein-tyrosine kinase.
PG  - 25512-9
AB  - Protein-tyrosine phosphatase 1B (PTP1B) is an important regulator of 
      protein-tyrosine kinase-dependent signaling pathways. Changes in expression and 
      activity of PTP1B have been associated with various human diseases; however, the 
      mechanisms by which PTP1B expression is regulated have yet to be characterized. 
      Previously, we have shown that the expression of PTP1B is enhanced by p210 
      Bcr-Abl and that PTP1B is a specific antagonist of transformation induced by this 
      oncoprotein protein-tyrosine kinase. Here we have characterized the PTP1B 
      promoter and demonstrate that a motif with features of a stress-response element 
      acts as a p210 Bcr-Abl-responsive sequence, termed PRS. We have shown that three 
      C(2)H(2) zinc finger proteins, namely Sp1, Sp3, and Egr-1, bind to PRS. Whereas 
      binding of either Sp1 or Sp3 induced promoter function, Egr-1 repressed 
      Sp3-mediated PTP1B promoter activation. The binding of Egr-1 to PRS is suppressed 
      by p210 Bcr-Abl due to the inhibition of Egr-1 expression, resulting in the 
      enhancement of PTP1B promoter activity. Our data indicate that Egr-1 and Sp 
      family proteins play a reciprocal role in the control of expression from the 
      PTP1B promoter.
FAU - Fukada, T
AU  - Fukada T
AD  - Cold Spring Harbor Laboratory, Demerec Bldg., 1 Bungtown Rd., Cold Spring Harbor, 
      NY 11724-2208, USA.
FAU - Tonks, N K
AU  - Tonks NK
LA  - eng
SI  - GENBANK/AY029236
GR  - CA53840/CA/NCI NIH HHS/United States
GR  - P30 CA45508/CA/NCI 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.
DEP - 20010420
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (EGR1 protein, human)
RN  - 0 (Early Growth Response Protein 1)
RN  - 0 (Immediate-Early Proteins)
RN  - 0 (SP3 protein, human)
RN  - 0 (Sp1 Transcription Factor)
RN  - 0 (Transcription Factors)
RN  - 148710-94-5 (Sp3 Transcription Factor)
RN  - EC 2.7.10.2 (Fusion Proteins, bcr-abl)
RN  - EC 3.1.3.48 (PTPN1 protein, human)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 1)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatases)
SB  - IM
MH  - Base Sequence
MH  - DNA-Binding Proteins/*physiology
MH  - Down-Regulation
MH  - Early Growth Response Protein 1
MH  - Fusion Proteins, bcr-abl/*metabolism
MH  - *Gene Expression Regulation
MH  - Humans
MH  - *Immediate-Early Proteins
MH  - Molecular Sequence Data
MH  - *Promoter Regions, Genetic
MH  - Protein Folding
MH  - Protein Tyrosine Phosphatase, Non-Receptor Type 1
MH  - Protein Tyrosine Phosphatases/*genetics
MH  - Sp1 Transcription Factor
MH  - Sp3 Transcription Factor
MH  - Transcription Factors/*physiology
MH  - Zinc Fingers
EDAT- 2001/04/24 10:00
MHDA- 2001/08/10 10:01
CRDT- 2001/04/24 10:00
PHST- 2001/04/24 10:00 [pubmed]
PHST- 2001/08/10 10:01 [medline]
PHST- 2001/04/24 10:00 [entrez]
AID - S0021-9258(20)79642-0 [pii]
AID - 10.1074/jbc.M101354200 [doi]
PST - ppublish
SO  - J Biol Chem. 2001 Jul 6;276(27):25512-9. doi: 10.1074/jbc.M101354200. Epub 2001 
      Apr 20.