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Blood, 1 August 2001, Vol. 98, No. 3, pp. 636-642
HEMATOPOIESIS
DUB-2A, a new member of the DUB subfamily of
hematopoietic deubiquitinating enzymes
Kwang-Hyun Baek,
Michelle
A. Mondoux,
Robert Jaster,
Ella Fire-Levin, and
Alan D. D'Andrea
From the Department of Pediatric Oncology, Dana-Farber
Cancer Institute, Harvard Medical School, Boston, MA.
Protein ubiquitination is an important regulator of
cytokine-activated signal transduction pathways and hematopoietic cell growth. Protein ubiquitination is controlled by the coordinate action
of ubiquitin-conjugating enzymes and deubiquitinating enzymes. Recently a novel family of genes encoding growth-regulatory
deubiquitinating enzymes (DUB-1 and DUB-2) has been identified.
DUBs are immediate-early genes and are induced rapidly and
transiently in response to cytokine stimuli. By means of polymerase
chain reaction amplification with degenerate primers for the
DUB-2 complementary DNA, 3 murine bacterial artificial
chromosome (BAC) clones that contain DUB gene sequences were isolated. One BAC contained a novel DUB gene
(DUB-2A) with extensive homology to DUB-2. Like
DUB-1 and DUB-2, the DUB-2A gene
consists of 2 exons. The predicted DUB-2A protein is highly related to
other DUBs throughout the primary amino acid sequence, with a
hypervariable region at its C-terminus. In vitro, DUB-2A had functional deubiquitinating activity; mutation of its conserved amino acid residues abolished this activity. The 5' flanking sequence of the DUB-2A gene has a hematopoietic-specific functional
enhancer sequence. It is proposed that there are at least 3 members of the DUB subfamily (DUB-1, DUB-2,
and DUB-2A) and that different hematopoietic cytokines
induce specific DUB genes, thereby initiating a
cytokine-specific growth response.
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