von Hippel-Lindau Partner Jade-1 Is a Transcriptional Co-activator Associated with Histone Acetyltransferase Activity

Panchenko, Mikhail P.; Zhou, Mina I.; Cohen, Herbert T.

doi:10.1074/jbc.m410487200

Cited by 43 publications

(90 citation statements)

References 42 publications

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“…For expression in bacteria, the different domains of JADE1, JADE3, ING4, ING5, HBO1, hEaf6, Yng2, and Esa1 were cloned by PCR into pGEX4T3 (GE Healthcare), pET15bϩ (Novagen), or pST44 (55), and the recombinant proteins were purified following standard procedures. Mammalian expression vectors for HA-and FLAG-tagged JADE1S (S stands for short) with amino acids 1 to 509 [JADE1S(1-509)] isoform and its PHD mutants have been described previously (40). For transient transfections, 2 ϫ 10 6 cells (HeLa S3, 293T, and RKO) were transfected with 8 g of each expression plasmid by the calcium phosphate method.…”

Section: Methodsmentioning

confidence: 99%

“…JADE1, a candidate tumor suppressor, has been physically linked to von Hippel-Lindau (VHL) function, transcription regulation, Wnt signaling, and apoptosis (6,40,(74)(75)(76). Our initial purification of HBO1 acetyltransferase complexes identified full-length JADE1/2/3 paralogues as stably associated subunits (8).…”

Section: Myst-ing Hat Complexes Can Be Separated Into Three Classesmentioning

confidence: 99%

“…2A) (12,53). In fact, the bulk of functional information on JADE1 in the literature is based on this smaller 509-amino-acid protein produced by an abundant mRNA splice variant (40,(74)(75)(76).…”

Section: Myst-ing Hat Complexes Can Be Separated Into Three Classesmentioning

confidence: 99%

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Conserved Molecular Interactions within the HBO1 Acetyltransferase Complexes Regulate Cell Proliferation

Avvakumov

Lalonde

Saksouk

et al. 2012

Molecular and Cellular Biology

128

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Acetyltransferase complexes of the MYST family with distinct substrate specificities and functions maintain a conserved association with different ING tumor suppressor proteins. ING complexes containing the HBO1 acetylase are a major source of histone H3 and H4 acetylation in vivo and play critical roles in gene regulation and DNA replication. Here, our molecular dissection of HBO1/ING complexes unravels the protein domains required for their assembly and function. Multiple PHD finger domains present in different subunits bind the histone H3 N-terminal tail with a distinct specificity toward lysine 4 methylation status. We show that natively regulated association of the ING4/5 PHD domain with HBO1-JADE determines the growth inhibitory function of the complex, linked to its tumor suppressor activity. Functional genomic analyses indicate that the p53 pathway is a main target of the complex, at least in part through direct transcription regulation at the initiation site of p21/CDKN1A. These results demonstrate the importance of ING association with MYST acetyltransferases in controlling cell proliferation, a regulated link that accounts for the reported tumor suppressor activities of these complexes. Members of the ING (inhibitor of growth) family of growth regulators are present in all eukaryotes, with the five human proteins (ING1 to ING5) and the three from Saccharomyces cerevisiae (Yng1, Yng2, and Pho23) being the most studied. Their homology is highest at the carboxyl termini within a plant homeodomain (PHD) finger-a motif common to many chromatin regulatory proteins (8, 54). Expression analyses of several tumor types show that ING genes are either mutated or downregulated in many forms of cancer (43,73), and a number of studies have implicated the ING proteins in the regulation of the cell cycle and proliferation, cellular aging and senescence, hormone signaling pathways, brain tumor growth, and angiogenesis (reviewed in reference 51). These functions stem from direct mechanistic roles in chromatin modification and remodeling, gene-specific transcription regulation, and DNA repair, recombination, and replication (2, 54, 61).The multisubunit protein complexes containing ING family members have been purified and characterized from yeast and human cells (reviewed in references 2 and 54). The human INGs can be divided into three groups-ING1/2, ING3, and ING4/5-based on their association with three distinct types of protein complexes (8). Each of these complexes regulates chromatin modification and structure via histone acetylation and deacetylation. The ING complexes that carry out histone acetylation contain members of the MYST family of histone acetyltransferases (HATs) as their catalytic subunits (Fig. 1A). Human MYST HATs include Tip60 (KAT5), HBO1 (KAT7), MOZ (KAT6A), MORF (KAT6B), and MOF (KAT8). These enzymes are also known to play crucial roles in transcription activation and in DNA repair, recombination, and replication and are implicated in development and many human diseases, most notably cancer (2,14,...

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Section: Methodsmentioning

confidence: 99%

Section: Myst-ing Hat Complexes Can Be Separated Into Three Classesmentioning

confidence: 99%

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Conserved Molecular Interactions within the HBO1 Acetyltransferase Complexes Regulate Cell Proliferation

Avvakumov

Lalonde

Saksouk

et al. 2012

Molecular and Cellular Biology

128

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“…The PHD finger domain is shared by various nuclear proteins and has been proposed to be involved in protein-protein interactions (Aasland et al, 1995). In animals, the PHD finger domain is known among transcriptional co-regulators and proteins in chromatin modifying complexes, such as Jade-1, p300, CBP and ING1 (Aasland et al, 1995;Bordoli et al, 2001;Feng et al, 2002;Panchenko et al, 2004) and constitutes a highly specialized trimethyl-lysine binding domain (Li et al, 2006;Peña et al, 2006;Shi et al, 2006;Wysocka et al, 2006). In plants, the PHD finger domain has been identified in MS1, MMD, EBS and VIN3, which are regarded as putative transcriptional regulators involved in fertility or flowering (Wilson et al, 2001;Pineiro et al, 2003;Yang et al, 2003;Sung and Amasino, 2004).…”

Section: Obe1 and Obe2 Encode Phd Finger Proteinsmentioning

confidence: 99%

TheArabidopsis OBERON1andOBERON2genes encode plant homeodomain finger proteins and are required for apical meristem maintenance

et al. 2008

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Maintenance of the stem cell population located at the apical meristems is essential for repetitive organ initiation during the development of higher plants. Here, we have characterized the roles of OBERON1 (OBE1) and its paralog OBERON2 (OBE2), which encode plant homeodomain finger proteins, in the maintenance and/or establishment of the meristems in Arabidopsis. Although the obe1 and obe2 single mutants were indistinguishable from wild-type plants, the obe1 obe2 double mutant displayed premature termination of the shoot meristem, suggesting that OBE1 and OBE2 function redundantly. Further analyses revealed that OBE1 and OBE2 allow the plant cells to acquire meristematic activity via the WUSCHEL-CLAVATA pathway, which is required for the maintenance of the stem cell population, and they function parallel to the SHOOT MERISTEMLESS gene, which is required for preventing cell differentiation in the shoot meristem. In addition, obe1 obe2 mutants failed to establish the root apical meristem, lacking both the initial cells and the quiescent center. In situ hybridization revealed that expression of PLETHORA and SCARECROW, which are required for stem cell specification and maintenance in the root meristem, was lost from obe1 obe2 mutant embryos. Taken together, these data suggest that the OBE1 and OBE2 genes are functionally redundant and crucial for the maintenance and/or establishment of both the shoot and root meristems.

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“…Human Jade is part of the HBO1 MYST HAT complex, whereas BRPF is a MOZ/ MORF complex component. Jade itself has close connections to human cancer, as it is reported to interact with the von Hippel-Lindau tumor suppressor as well as human Tip60 (Zhou et al, 2002;Panchenko et al, 2004).…”

Section: Parallels In Myst Complexesmentioning

confidence: 99%

MYST opportunities for growth control: yeast genes illuminate human cancer gene functions

et al. 2007

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The MYST family of histone acetyltransferases (HATs) was initially defined by human genes with disease connections and by yeast genes identified for their role in epigenetic transcriptional silencing. Since then, many new MYST genes have been discovered through genetic and genomic approaches. Characterization of the complexes through which MYST proteins act, regions of the genome to which they are targeted and biological consequences when they are disrupted, all deepen the connections of MYST proteins to development, growth control and human cancers. Many of the insights into MYST family function have come from studies in model organisms. Herein, we review functions of two of the founding MYST genes, yeast SAS2 and SAS3, and the essential yeast MYST ESA1. Analysis of these genes in yeast has defined roles for MYST proteins in transcriptional activation and silencing, and chromatin-mediated boundary formation. They have further roles in DNA damage repair and nuclear integrity. The observation that MYST protein complexes share subunits with other HATs, histone deacetylases and other key nuclear proteins, many with connections to human cancers, strengthens the idea that coordinating distinct chromatin modifications is critical for regulation.

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von Hippel-Lindau Partner Jade-1 Is a Transcriptional Co-activator Associated with Histone Acetyltransferase Activity

Cited by 43 publications

References 42 publications

Conserved Molecular Interactions within the HBO1 Acetyltransferase Complexes Regulate Cell Proliferation

Conserved Molecular Interactions within the HBO1 Acetyltransferase Complexes Regulate Cell Proliferation

TheArabidopsis OBERON1andOBERON2genes encode plant homeodomain finger proteins and are required for apical meristem maintenance

MYST opportunities for growth control: yeast genes illuminate human cancer gene functions

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