TALE homeoproteins as HOX11-interacting partners in T-cell leukemia (Q28187803)

Deregulation of a Homeobox Gene, HOX11, by the t(10;14) in T Cell Leukemia

Europe PubMed Central

title

TALE homeoproteins as HOX11-interacting partners in T-cell leukemia (English)

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T D Allen

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Y X Zhu

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2

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T S Hawley

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3

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R G Hawley

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4

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language of work or name

English

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publication date

October 2000

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published in

Leukemia & Lymphoma

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volume

39

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issue

3-4

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page(s)

241-56

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cites work

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The HOX11 gene encodes a DNA-binding nuclear transcription factor belonging to a distinct family of homeobox genes

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Fusion of the nucleoporin gene NUP98 to HOXA9 by the chromosome translocation t(7;11)(p15;p15) in human myeloid leukaemia

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The t(7;11)(p15;p15) translocation in acute myeloid leukaemia fuses the genes for nucleoporin NUP98 and class I homeoprotein HOXA9

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A new homeobox gene contributes the DNA binding domain of the t(1;19) translocation protein in pre-B ALL

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Meis1 and pKnox1 bind DNA cooperatively with Pbx1 utilizing an interaction surface disrupted in oncoprotein E2a-Pbx1

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Rapid detection of octamer binding proteins with 'mini-extracts', prepared from a small number of cells

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Pbx proteins display hexapeptide-dependent cooperative DNA binding with a subset of Hox proteins

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HOX11 interacts with protein phosphatases PP2A and PP1 and disrupts a G2/M cell-cycle checkpoint

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The PBX-regulating protein PREP1 is present in different PBX-complexed forms in mouse

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Dysregulation of HOX11 by chromosome translocations in T-cell acute lymphoblastic leukemia: a paradigm for homeobox gene involvement in human cancer

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Hoxa9 transforms primary bone marrow cells through specific collaboration with Meis1a but not Pbx1b

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AbdB-like Hox proteins stabilize DNA binding by the Meis1 homeodomain proteins

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HOXA9 forms triple complexes with PBX2 and MEIS1 in myeloid cells

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PBX and MEIS as non-DNA-binding partners in trimeric complexes with HOX proteins

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HoxA9-mediated immortalization of myeloid progenitors requires functional interactions with TALE cofactors Pbx and Meis

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The hexapeptide LFPWMR in Hoxb-8 is required for cooperative DNA binding with Pbx1 and Pbx2 proteins

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The optimal binding sequence of the Hox11 protein contains a predicted recognition core motif

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Pbx modulation of Hox homeodomain amino-terminal arms establishes different DNA-binding specificities across the Hox locus

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Cellular proliferation and transformation induced by HOXB4 and HOXB3 proteins involves cooperation with PBX1.

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The T-cell oncogenic protein HOX11 activates Aldh1 expression in NIH 3T3 cells but represses its expression in mouse spleen development

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Optimal activation of an endogenous gene by HOX11 requires the NH2-terminal 50 amino acids

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The pancreatic islet factor STF-1 binds cooperatively with Pbx to a regulatory element in the somatostatin promoter: importance of the FPWMK motif and of the homeodomain

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Pbx-1 Hox heterodimers bind DNA on inseparable half-sites that permit intrinsic DNA binding specificity of the Hox partner at nucleotides 3' to a TAAT motif.

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Distinct HOX N-terminal arm residues are responsible for specificity of DNA recognition by HOX monomers and HOX.PBX heterodimers

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Hox11 controls the genesis of the spleen

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