Jun 4, 2009 · Ectopic LMO2 expression causes leukemia in T-cell acute lymphoblastic leukemia (T-ALL) patients and severe combined immunodeficiency patients undergoing retroviral gene therapy. Tightly controlled Lmo2 expression is therefore essential, yet no comprehensive analysis of Lmo2 regulation has been published so far.

Jan 10, 2013 · LMO2 seems to function primarily through forming transcription factor complexes with TAL1 or LYL1, GATA proteins, LDB1, and E12 or E47 to regulate gene expression.

The most significant overlap was with targets of E12, an E2A protein demonstrated to be part of the LMO2 complex, 12 thus corroborating our coimmunoprecipitation and reporter results in B lymphoma cells.

Nov 11, 2013 · Here, we report the characterization of an enhancer responsible for Lmo2 expression in the embryonic tail bud and limbs. Using extensive transgenic mouse analysis, we demonstrate that this enhancer depends upon highly conserved HOX and E-box motifs.

Jan 4, 2000 · The LMO2 gene is activated by chromosomal translocations in human T cell acute leukemias, but in mouse embryogenesis, Lmo2 is essential for initiation of yolk sac and definitive hematopoiesis. The ...

Nov 1, 2007 · LMO2 belongs to a multigene family, extremely well conserved during evolution, encoding proteins containing two cystein-rich regions referred to as LIM domains: LMO1 (11p15), LMO2 (11p13), LMO3 (12p); 6 exons.

Feb 17, 2011 · Through its LIM domains, LMO2 is thought to function as the scaffold for a DNA-binding transcription regulator complex, including the basic helix-loop-helix proteins SCL/TAL1 and E47, the zinc finger protein GATA-1, and LIM-domain interacting protein LDB1.

TAL1 and LMO2 operate within multifactorial protein–DNA complexes that regulate gene expression in the developing blood cell. TAL1 is a tissue-specific basic helix–loop–helix (bHLH) protein that binds bHLH domains of ubiquitous E-proteins, (E12 and E47), to bind E-box (CANNTG) DNA motifs.

Aug 17, 1998 · Isolation of DNA‐binding sites by CASTing and band shift assays demonstrates the presence of an oligomeric complex involving Lmo2 which can bind to a bipartite DNA motif comprising two E‐box sequences ∼10 bp apart, which is distinct from that found in erythroid cells.

The Ldb1, LMO2, SCL/E12 Multiprotein Complex Recognizes the SCL E-Box DNA-Binding Motif. The potential involvement of Ldb1 in binding the SCL consensus E-box motif was evaluated by gel shift analysis of nuclear extracts prepared from transfected cells.