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Papers In Press, published online ahead of print August 1, 2001
J. Biol. Chem, 10.1074/jbc.M103381200
Submitted on April 16, 2001
Revised on July 29, 2001
Accepted on August 1, 2001
Medicine (Hematology/Oncology), Northwestern University Medical School and, Chicago, Illinois 60611
Corresponding Author: e-eklund{at}northwestern.edu
The CYBB and NCF2 genes encode the phagocyte respiratory burst oxidase proteins, gp91phox and p67phox. Previously, we identified homologous CYBB and NCF2 cis elements that are necessary for lineage specific transcription, during late myeloid differentiation. We determined that these homologous cis elements are activated by PU.1, IRF1, ICSBP and the CREB-binding protein (CBP). Since expression of PU.1 and ICSBP is lineage restricted, our investigations identified a mechanism of lineage specific CYBB and NCF2 transcription. Since PU.1, IRF1, ICSBP and CBP are expressed in undifferentiated myeloid cells, our investigations did not determine the mechanism of differentiation stage specific CYBB and NCF2 transcription. In the current investigations, we determine that SHP1 protein tyrosine phosphatase (SHP1-PTP) inhibits gp91phox and p67phox expression, in undifferentiated myeloid cell lines, by decreasing interaction of PU.1, IRF1, ICSBP and CBP with the CYBB and NCF2 genes. We also determine that IRF1 and ICSBP are tyrosine phosphorylated during IFN-differentiation of myeloid cell lines, and identify IRF1 and ICSBP tyrosine residues that are necessary for CYBB and NCF2 transcription. Therefore, these investigations identify a novel mechanism by which SHP1-PTP antagonizes myeloid differentiation, and determine that tyrosine phosphorylation of IRF1 and ICSPB mediates stage specific transcriptional activation in differentiating myeloid cells.
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