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Human Monoclonal MYST3 Primary Antibody for ChIP, IP - ABIN2668559
Paggetti, Largeot, Aucagne, Jacquel, Lagrange, Yang, Solary, Bastie, Delva: Crosstalk between leukemia-associated proteins MOZ and MLL regulates HOX gene expression in human cord blood CD34+ cells. in Oncogene 2010
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Human Polyclonal MYST3 Primary Antibody for ELISA - ABIN4234137
Rokudai, Aikawa, Tagata, Tsuchida, Taya, Kitabayashi: Monocytic leukemia zinc finger (MOZ) interacts with p53 to induce p21 expression and cell-cycle arrest. in The Journal of biological chemistry 2008
Histone acetyltransferase sactivity of Moz regulates homeobox expression and segsmental identity.
Results show that Moz and Hox genes function in cranial neural crest cells, but not in the ectoderm or endoderm, to specify the support skeleton.
the first inherited variant in KAT6A and suggest missense variants in KAT6A to be associated with an inheritable, milder clinical presentation compared to previously reported de novo, truncating mutations in this gene.
Overexpression of KAT6A or TRIM24 promoted PIK3CA expression, AKT phosphorylation, and cell proliferation.
Given the similar findings in animal models and our patient's phenotypes, we hypothesize that KAT6A could play a role in development of the brain, face, and heart in humans
MYST3 binds to the proximal promoter region of ERalpha gene, and inactivating mutations in its HAT domain abolished its ability to regulate ERalpha, suggesting MYST3 functioning as a histone acetyltransferase that activates ERalpha promoter.
Studies show that misregulation of MOZ/MORF results in tumorigenesis and developmental disorders. Results also provide evidence that these 2 proteins play important role in regulating cell proliferation and stem cell maintenance. [review]
The demonstrate that the histone acetylation-binding double PHD finger (DPF) domains of human MOZ (also known as KAT6A) and DPF2 (also known as BAF45d) accommodate a wide range of histone lysine acylation with the strongest preference for propionylation (Kcr).
In this study we report the frequency of FGFR1 and KAT6A involvement in patients with hematological malignancies and 8p11 abnormalities.
These data suggest that KAT6A may be a novel oncogene in breast cancers bearing the 8p11-p12 amplicon.
findings establish that MOZ and BMI1 play opposing roles during the onset of Hox gene expression in the ES cell model and during body segment identity specification in vivo.
We have identified KAT6A mutations as a frequent cause of syndromic developmental delay with microcephaly and dysmorphic features.
Heterozygous truncating mutations in KAT6A, as well as deletions of the same locus, cause a syndrome characterized by intellectual disability, craniosynostosis, cardiac defects, feeding difficulties, and distinct facial features.
MOZ-TIF2/BRPF1 complex upregulates HOX genes mediated by MOZ-dependent histone acetylation, leading to the development of leukemia.
The double PHD finger domain of MOZ/MYST3 induces alpha-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification.
Symplekin interacts and co-localizes with both MOZ and MLL in immature hematopoietic cells. Its inhibition leads to a decrease of the HOXA9 protein level but not of Hoxa9 mRNA.
Studies indicate the critical function of MOZ (MYST3 or KAT6A(1)) in haematopoiesis.
MYST3-CREBBP rearrangement harbors a distinctive microRNA signature targeting RET proto-oncogene in acute myeloid leukemia with translocation (8;16)(p11;p13).
MOZ is an acetyltransferase of p53 at K120 and K382 and colocalizes with p53 in promyelocytic leukemia (PML) nuclear bodies following cellular stress.
These data suggest that the tandem of plant homeodomain 1/2 fingers play a role in MOZ and MORF histone acetyltransferase association with histon H3 regions enriched in acetylated marks.
PHD12 facilitates the localization of MOZ onto the promoter locus of the HOXA9 gene, thereby promoting the H3 acetylation around the promoter region.
Recognition of unmodified histone H3 by the first PHD finger of bromodomain-PHD finger protein 2 provides insights into the regulation of histone acetyltransferases monocytic leukemic zinc-finger protein (MOZ) and MOZ-related factor (MORF).
Loss of MOZ in adult mice leads to the rapid loss of hematopoietic stem cells as defined by transplantation.
Our work revealed that MOZ and BMI1 regulate HSCs in a synergistic manner by acting on distinct processes required to maintain HSCs.
BRPF2-MOZ complexes play an important role in the differentiation of embryonic stem cells via H3K14 acetylation.
the expression of MOZ-TIF2 fusion protein represses the transcription of p16INK4a and p19ARF and blocks senescence.
Study establishes that MOZ is an upstream inhibitor of the INK4A-ARF pathway, and suggests that inhibiting MOZ may be one way to induce senescence in proliferative tumor cells.
these data suggest that the molecular pathogenesis of ventricular septal defectss in Moz germline mutant mice is due to loss of MOZ-dependant activation of mesodermal Tbx1 and Tbx5 expression.
MOZ regulates B-cell progenitors and, consequently, Moz haploinsufficiency dramatically retards MYC-induced lymphoma development
These results suggest a critical requirement for MOZ HAT activity to silence p16(INK4a) expression and to protect stem cells from early entrance into replicative senescence.
MOZ regulates B-cell memory formation, controlling memory compartment composition, an activity that is B cell-intrinsic and required for establishing the germinal center gene expression program.
MOZ interacts with the gene Tbx1 which influences heart and aortic arch development and is involved in DiGeorge syndrome.
The show that lack of the histone acetyltransferase MOZ (MYST3/KAT6A) phenocopies DiGeorge syndrome, and the MOZ complex occupies the Tbx1 locus, promoting its expression and histone 3 lysine 9 acetylation.
Moz is essential for a fundamental property of hematopoietic stem cells, the ability to reconstitute the hematopoietic system of a recipient after transplantation and that Moz is specifically required in the stem cell compartment.
MOZ is required for maintenance of hematopoietic stem cells, and that it plays a role in differentiation of erythroid and myeloid cells.
Monocytic leukemia zinc finger (MOZ) interacts with p53 to induce p21 expression and cell-cycle arrest.
A specific role of MOZ-driven acetylation in controlling a desirable balance between proliferation and differentiation during hematopoiesis.
data show that Moz regulates H3K9 acetylation at Hox gene loci and that retinoic acid can act independently of Moz to establish specific Hox gene expression boundaries.
Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2 (By similarity).
MYST histone acetyltransferase (monocytic leukemia) 3
, histone acetyltransferase MYST3
, monocytic leukemia zinc finger protein
, histone acetyltransferase MYST3-like
, K(lysine) acetyltransferase 6A
, MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3
, Monocytic leukemia zinc finger protein
, histone acetyltransferase KAT6A
, runt-related transcription factor binding protein 2
, runt-related transcription factor-binding protein 2
, zinc finger protein 220
, monocytic leukemia zinc finger homolog
, MYST protein 3