P. P. Pandolfi (auth.), Pier Paolo Pandolfi MD, Ph.D., Peter's Acute Promyelocytic Leukemia: Molecular Genetics, Mouse PDF

By P. P. Pandolfi (auth.), Pier Paolo Pandolfi MD, Ph.D., Peter K. Vogt Ph.D. (eds.)

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McConnell · J. D. Licht There is a growing body of evidence that, in addition to the nucleus, PLZF can be found in the cytoplasm. In a process called “ectodomain shedding,” a membrane-anchored ligand for the epidermal growth factor receptor (EGFR) HB-EGF (heparin-binding EGF-like growth factor) is cleaved, generating a small, roughly 7-kDa fragment of HB-EGF in the cytoplasm of the cell. This translocates to the nucleus where it binds PLZF through the first three (N-terminal) zinc fingers of PLZF [60, 61].

This fusion protein binds the same DNA sequences as PLZF, but does not have the PLZF repression domains. RARα-PLZF is an oncogenic version of PLZF, The PLZF Gene of t(11;17)-Associated APL 33 likely activating transcription of genes that are normally repressed by PLZF, due to the replacement of the PLZF repression domains with the activation domains of RARα. Regulation and control of PLZF expression is incompletely understood. The gene is expressed in distinct temporal and spatial patterns in multiple tissues, both during embryogenesis and in the adult, but the factors that control these patterns have not been identified.

We found that transcriptional repression by PLZF was inhibited by co-expression of a mutant, constitutively active form of the tyrosine kinase receptor Flt3. Flt3 is the most common mutation identified in human leukemia and mediates signaling through the ras-mitogen-activated protein (MAP) kinase pathway as well as through the Janus kinase/signal transducer and activator of transcription (JAK-STAT) pathway [19]. Co-expression of constitutively activated ras or stress kinases also blocks transcriptional repression by PLZF [32, 82].

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