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健治, 滝; 玲児, 涌沢

doi:10.3925/jjtc1958.28.359

Cited by 27 publications

(35 citation statements)

References 12 publications

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“…Similarly, it is also involved in the activity of members of the nuclear receptor family (Chen et al, 1997;Kamei et al, 1996;Torchia et al, 1997), some of which are likewise potent inhibitors of cell proliferation. In addition, p300 mutations have been described in two cases of human tumours; and CBP is a component of fusion proteins causative of some leukaemias (Muraoka et al, 1996;Satake et al, 1997;Taki et al, 1997). Finally, in a few examples p300 has been shown to repress cell transformation, for example by E1A (Smits et al, 1996).…”

Section: Discussionmentioning

confidence: 99%

CBP/p300 histone acetyl-transferase activity is important for the G1/S transition

et al. 2000

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Transforming viral proteins such as E1A which force quiescent cells into S phase have two essential cellular target proteins, Rb and CBP/p300. Rb regulates the G1/ S transition by controlling the transcription factor E2F. CBP/p300 is a transcriptional co-activator with intrinsic histone acetyl-transferase activity. This activity is regulated in a cell cycle dependent manner and shows a peak at the G1/S transition, suggesting a function for CBP/p300 in this crucial step of the cell cycle. Here, we have arti®cially modulated CBP/p300 levels in individual cells through microinjection of speci®c antibodies and expression vectors. We show that CBP/p300 is required for cell proliferation and has an essential function during the G1/S transition. Using the same microinjection system and GFP-reporter vectors, we demonstrate that CBP/p300 is essential for the activity of E2F, a transcription factor that controls the G1/S transition. In addition, our results suggest that CBP HAT activity is required both for the G1/S transition and for E2F activity. Thus CBP/p300 seems to be a versatile protein involved in opposing cellular processes, which raises the question of how its multiple activities are regulated.

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Section: Discussionmentioning

confidence: 99%

CBP/p300 histone acetyl-transferase activity is important for the G1/S transition

et al. 2000

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“…Analogous to DNA-binding transcription factors, these coactivators are also frequent targets of cancer-associated chromosomal rearrangements. Consistent with this notion, leukemia-associated chromosomal translocations have been found to alter the well-known transcriptional coactivators CBP and p300 (Borrow et al, 1996;Ida et al, 1997;Rowley et al, 1997;Satake et al, 1997;Sobulo et al, 1997;Taki et al, 1997;Chaanet et al, 1999Chaanet et al, , 2000Jacobson and Pillus, 1999;Lavau et al, 2000;Panagopoulos et al, 2000;Kitabayashi et al, 2001b). For example, their genes were discovered to be rearranged in the reciprocal translocations t(8;16)(p11;q13) and t(8;22)(p11;q13), respectively (Borrow et al, 1996;Chaanet et al, 1999Chaanet et al, , 2000Panagopoulos et al, 2000).…”

Section: Introductionmentioning

confidence: 90%

MOZ and MORF histone acetyltransferases interact with the Runt-domain transcription factor Runx2

et al. 2002

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The monocytic leukemia zinc ®nger protein MOZ and its homologue MORF have been implicated in leukemogenesis. Both MOZ and MORF are histone acetyltransferases with weak transcriptional repression domains and strong transcriptional activation domains, suggesting that they may function as transcriptional coregulators. Here we describe that MOZ and MORF both interact with Runx2 (or Cbfa1), a Runt-domain transcription factor that is known to play important roles in T cell lymphomagenesis and bone development. Through its C-terminal SM (serine-and methioninerich) domain, MORF binds to Runx2 in vitro and in vivo. Consistent with this, the SM domain of MORF also binds to Runx1 (or AML1), a Runx2 homologue that is frequently altered by leukemia-associated chromosomal translocations. While MORF does not acetylate Runx2, its SM domain potentiates Runx2-dependent transcriptional activation. Moreover, endogenous MORF is required for transcriptional activation by Runx2. Intriguingly, Runx2 negatively regulates the transcriptional activation potential of the SM domain. Like that of MORF, the SM domain of MOZ physically and functionally interacts with Runx2. These results thus identify Runx2 as an interaction partner of MOZ and MORF and suggest that both acetyltransferases are involved in regulating transcriptional activation mediated by Runx2 and its homologues.

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“…Several MLL fusions with nuclear transcription factors (Corral et al, 1996;Lavau et al, 1997) or with proteins central to transcriptional regulation (Lavau et al, 2000a,b) transform hematopoietic progenitors (Lavau et al, 1997(Lavau et al, , 2000a, and/or are leukaemogenic in transgenic mice (Corral et al, 1996) or in mouse models created by retroviral-mediated gene transfer (Lavau et al, 1997(Lavau et al, , 2000a. Whereas many MLL partner proteins have structural motifs of nuclear transcription factors (LAF-4, AF4, AF5a, AF5q31, AF6q21, AF9, AF10, MLL, AF17, ENL, AFX) Chaplin et al, 1995;Gu et al, 1992;Hillion et al, 1997;Morrissey et al, 1993;Nakamura et al, 1993;Prasad et al, 1994;Schichman et al, 1994;Taki et al, 1996Taki et al, , 1999aTkachuk et al, 1992), proteins involved in transcriptional regulation (CBP, ELL, p300) (Ida et al, 1997;Sobulo et al, 1997;Taki et al, 1997;Thirman et al, 1994) or, in one case, a nuclear protein of unknown function (AF15q14) (Hayette et al, 2000), other MLL partner proteins are found in the cytoplasm (AF1p, AF1q, AF3p21, GMPS, LPP, GRAF, FBP17, ABI-1, GAS7, EEN) (Bernard et al, 1994;Borkhardt et al, 2000;Daheron et al, 2001;Fuchs et al, 2001;Megonigal et al, 2000a;Pegram et al, 2000;Sano et al, 2000;So et al, 1997;Taki et al, 1998;Tse et al, 1995) or at the cell membrane (AF6, LARG, GPHN) (Eguchi et al, 2001;…”

Section: Introductionmentioning

confidence: 99%

MLL-SEPTIN6 fusion recurs in novel translocation of chromosomes 3, X, and 11 in infant acute myelomonocytic leukaemia and in t(X;11) in infant acute myeloid leukaemia, and MLL genomic breakpoint in complex MLL-SEPTIN6 rearrangement is a DNA topoisomerase II cleavage site

et al. 2002

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We examined the MLL translocation in two cases of infant AML with X chromosome disruption. The Gbanded karyotype in the first case suggested t(X;3)(q22;p21)ins(X;11)(q22;q13q25). Southern blot analysis showed one MLL rearrangement. Panhandle PCR approaches were used to identify the MLL fusion transcript and MLL genomic breakpoint junction. SEPTIN6 from chromosome band Xq24 was the partner gene of MLL. MLL exon 7 was joined in-frame to SEPTIN6 exon 2 in the fusion transcript. The MLL genomic breakpoint was in intron 7; the SEPTIN6 genomic breakpoint was in intron 1. Spectral karyotyping revealed a complex rearrangement disrupting band 11q23. FISH with a probe for MLL confirmed MLL involvement and showed that the MLL-SEPTIN6 junction was on the der(X). The MLL genomic breakpoint was a functional DNA topoisomerase II cleavage site in an in vitro assay. In the second case, the karyotype revealed t(X;11)(q22;q23). Southern blot analysis showed two MLL rearrangements. cDNA panhandle PCR detected a transcript fusing MLL exon 8 in-frame to SEPTIN6 exon 2. MLL and SEPTIN6 are vulnerable to damage to form recurrent translocations in infant AML. Identification of SEPTIN6 and the SEPTIN family members hCDCrel and MSF as partner genes of MLL suggests a common pathway to leukaemogenesis.

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Cited by 27 publications

References 12 publications

CBP/p300 histone acetyl-transferase activity is important for the G1/S transition

CBP/p300 histone acetyl-transferase activity is important for the G1/S transition

MOZ and MORF histone acetyltransferases interact with the Runt-domain transcription factor Runx2

MLL-SEPTIN6 fusion recurs in novel translocation of chromosomes 3, X, and 11 in infant acute myelomonocytic leukaemia and in t(X;11) in infant acute myeloid leukaemia, and MLL genomic breakpoint in complex MLL-SEPTIN6 rearrangement is a DNA topoisomerase II cleavage site

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