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Prepublished online as a Blood First Edition Paper on October 17, 2002; DOI 10.1182/blood-2002-08-2652.
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Blood, 1 March 2003, Vol. 101, No. 5, pp. 1934-1940
NEOPLASIA
Evi3, a common retroviral integration site in murine
B-cell lymphoma, encodes an EBFAZ-related Krüppel-like zinc
finger protein
Søren Warming,
Pentao Liu,
Takeshi Suzuki,
Keiko Akagi,
Susan Lindtner,
George N. Pavlakis,
Nancy A. Jenkins, and
Neal G. Copeland
From the Mouse Cancer Genetics Program and the Basic
Research Laboratory, National Cancer Institute, Frederick, MD.
Retroviral insertional mutagenesis in inbred mouse strains provides
a powerful method for cancer gene discovery. Here, we show that a
common retroviral integration site (RIS) in AKXD B-cell lymphomas,
termed Evi3, encodes a novel zinc finger protein with 30 Krüppel-like zinc finger repeats. Most integrations at
Evi3 are located upstream of the first translated exon and
result in 3' long-terminal repeat (LTR)-driven overexpression of
Evi3. Evi3 is highly related to the early
B-cell factor-associated zinc finger gene (Ebfaz), and all
30 zinc fingers found in EVI3 are conserved in EBFAZ. EBFAZ binds to
and negatively regulates early B-cell factor (EBF) (also known as
olfactory-1, OLF1), a basic helix-loop-helix (bHLH)
transcription factor required for B-lineage commitment and the
development of the olfactory epithelium. EBFAZ also binds to SMA- and
MAD-related protein-1 (SMAD1) and SMAD4 in response to bone
morphogenetic protein-2 (BMP2) signaling, which in turn activates the homeobox regulator of Xenopus mesoderm and neural development Xvent-2. Surprisingly, while Ebfaz
and Evi3 are coexpressed in many tissues, and both proteins
are nuclear, we could not detect Ebfaz expression in B
cells by reverse transcriptase-polymerase chain reaction
(RT-PCR), whereas Evi3 expression could be detected at all stages of B-cell development. Our results suggest that EVI3,
like EBFAZ, is a multifunctional protein that participates in many
signaling pathways via its multiple zinc fingers. Furthermore, our
results suggest that EVI3, not EBFAZ, is the member of this protein
family that interacts with and regulates EBF in B cells.
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