The Experts below are selected from a list of 32835 Experts worldwide ranked by ideXlab platform
Anthony N Imbalzano - One of the best experts on this subject based on the ideXlab platform.
-
ck2 dependent phosphorylation of the brg1 Chromatin Remodeling enzyme occurs during mitosis
bioRxiv, 2019Co-Authors: Teresita Padillabenavides, Dominic T Haokip, Yeonsoo Yoon, Pablo Reyesgutierrez, Jaime A Riveraperez, Anthony N ImbalzanoAbstract:ABSTRACT Brg1 (Brahma related gene 1) is one of two mutually exclusive ATPases that can act as the catalytic subunit of mammalian SWI/SNF Chromatin Remodeling enzymes that facilitate utilization of the DNA in eukaryotic cells. Brg1 is a phospho-protein and its activity is regulated by specific kinases and phosphatases. Previously, we showed that Brg1 interacts with and is phosphorylated by casein kinase 2 (CK2) in a manner that regulates myoblast proliferation. Here we demonstrate that the Brg1-CK2 interaction occurred during mitosis in embryonic somites and in primary myoblasts derived from satellite cells isolated from muscle tissue. The interaction of CK2 activity with Brg1 and the incorporation of a number of other subunits into the mSWI/SNF enzyme complex were independent of CK2 enzymatic activity. CK2-mediated hyperphosphorylation of Brg1 was observed in mitotic cells derived from multiple cell types and organisms, suggesting functional conservation across tissues and species. The mitotically hyperphosphorylated form of Brg1 was localized with soluble Chromatin, demonstrating that CK2-mediated phosphorylation of Brg1 is associated with specific partitioning of Brg1 within sub-cellular compartments. Thus CK2 acts a mitotic kinase that regulates Brg1 phosphorylation and sub-cellular localization. HIGHLIGHTS Interactions between CK2 and the Brg1 Chromatin Remodeling enzyme occur during mitosis CK2-Brg1 interactions are independent of CK2 catalytic activity CK2-mediated phosphorylation of Brg1 is a mitotic event CK2-mediated phosphorylation of Brg1 is conserved across mammalian cell types The mitotically hyperphosphorylated form of Brg1 is localized with soluble Chromatin
-
the protein arginine methyltransferase prmt5 is required for myogenesis because it facilitates atp dependent Chromatin Remodeling
Molecular and Cellular Biology, 2007Co-Authors: Caroline S Dacwag, Said Sif, Yasuyuki Ohkawa, Sharmistha Pal, Anthony N ImbalzanoAbstract:Skeletal muscle differentiation requires the coordinated activity of transcription factors, histone modifying enzymes, and ATP-dependent Chromatin Remodeling enzymes. The type II protein arginine methyltransferase Prmt5 symmetrically dimethylates histones H3 and H4 and numerous nonChromatin proteins, and prior work has implicated Prmt5 in transcriptional repression. Here we demonstrate that MyoD-induced muscle differentiation requires Prmt5. One of the first genes activated during differentiation encodes the myogenic regulator myogenin. Prmt5 and dimethylated H3R8 (histone 3 arginine 8) are localized at the myogenin promoter in differentiating cells. Modification of H3R8 required Prmt5, and reduction of Prmt5 resulted in the abrogation of promoter binding by the Brg1 ATPase-associated with the SWI/SNF Chromatin Remodeling enzymes and all subsequent events associated with gene activation, including increases in Chromatin accessibility and stable binding by MyoD. Prmt5 and dimethylated H3R8 were also associated with the myogenin promoter in activated satellite cells isolated from muscle tissue, further demonstrating the physiological relevance of these observations. The data indicate that Prmt5 facilitates myogenesis because it is required for Brg1-dependent Chromatin Remodeling and gene activation at a locus essential for differentiation. We therefore conclude that a histone modifying enzyme is necessary to permit an ATP-dependent Chromatin Remodeling enzyme to function. Gene expression is a highly regulated process that frequently requires coordinated function between transcription factors and Chromatin Remodeling enzymes. These enzymes are divided into two classes: ATP-dependent remodelers that hydrolyze ATP and alter nucleosome structure and histone modifiers that covalently modify specific histone residues posttranslationally. The activation of skeletal muscle differentiation is regulated by members of the basic helix-loop-helix family of tissue-specific transcription factors, including MyoD, Myf5, Mrf4, and myogenin, as well as by members of the Mef2 family of transcriptional regulators, which act cooperatively with basic helix-loop-helix proteins (8, 34, 43). Numerous Chromatin Remodeling enzymes have been shown to both positively and negatively affect myogenic gene expression. These include histone acetyl transferases; types I, II; and III histone deacetylases; histone lysine methyltransferases; and members of the SWI/SNF family of ATP-dependent Remodeling enzymes (17, 47, 50). The relationships between the different classes of Chromatin Remodeling enzymes during myogenesis have been largely unexplored. The protein arginine methyltransferases (PRMTs) are an additional class of enzymes that can be linked to histone modification and gene regulation during skeletal muscle differentiation. This family has 9 members (Prmt1 to Prmt9), six of
-
the protein arginine methyltransferase prmt5 is required for myogenesis because it facilitates atp dependent Chromatin Remodeling
Molecular and Cellular Biology, 2007Co-Authors: Caroline S Dacwag, Said Sif, Yasuyuki Ohkawa, Sharmistha Pal, Anthony N ImbalzanoAbstract:Skeletal muscle differentiation requires the coordinated activity of transcription factors, histone modifying enzymes, and ATP-dependent Chromatin Remodeling enzymes. The type II protein arginine methyltransferase Prmt5 symmetrically dimethylates histones H3 and H4 and numerous nonChromatin proteins, and prior work has implicated Prmt5 in transcriptional repression. Here we demonstrate that MyoD-induced muscle differentiation requires Prmt5. One of the first genes activated during differentiation encodes the myogenic regulator myogenin. Prmt5 and dimethylated H3R8 (histone 3 arginine 8) are localized at the myogenin promoter in differentiating cells. Modification of H3R8 required Prmt5, and reduction of Prmt5 resulted in the abrogation of promoter binding by the Brg1 ATPase-associated with the SWI/SNF Chromatin Remodeling enzymes and all subsequent events associated with gene activation, including increases in Chromatin accessibility and stable binding by MyoD. Prmt5 and dimethylated H3R8 were also associated with the myogenin promoter in activated satellite cells isolated from muscle tissue, further demonstrating the physiological relevance of these observations. The data indicate that Prmt5 facilitates myogenesis because it is required for Brg1-dependent Chromatin Remodeling and gene activation at a locus essential for differentiation. We therefore conclude that a histone modifying enzyme is necessary to permit an ATP-dependent Chromatin Remodeling enzyme to function.
Kyosuke Nagata - One of the best experts on this subject based on the ideXlab platform.
-
function of homo and hetero oligomers of human nucleoplasmin nucleophosmin family proteins npm1 npm2 and npm3 during sperm Chromatin Remodeling
Nucleic Acids Research, 2012Co-Authors: Mitsuru Okuwaki, Ayako Sumi, Miharu Hisaoka, Ai Saotomenakamura, Satoko Akashi, Yoshifumi Nishimura, Kyosuke NagataAbstract:Sperm Chromatin Remodeling after oocyte entry is the essential step that initiates embryogenesis. This reaction involves the removal of sperm-specific basic proteins and Chromatin assembly with histones. In mammals, three nucleoplasmin/nucleophosmin (NPM) family proteins–NPM1, NPM2 and NPM3–expressed in oocytes are presumed to cooperatively regulate sperm Chromatin Remodeling. We characterized the sperm Chromatin decondensation and nucleosome assembly activities of three human NPM proteins. NPM1 and NPM2 mediated nucleosome assembly independently of other NPM proteins, whereas the function of NPM3 was largely dependent on formation of a complex with NPM1. Maximal sperm Chromatin Remodeling activity of NPM2 required the inhibition of its non-specific nucleic acid-binding activity by phosphorylation. Furthermore, the oligomer formation with NPM1 elicited NPM3 nucleosome assembly and sperm Chromatin decondensation activity. NPM3 also suppressed the RNA-binding activity of NPM1, which enhanced the nucleoplasm–nucleolus shuttling of NPM1 in somatic cell nuclei. Our results proposed a novel mechanism whereby three NPM proteins cooperatively regulate Chromatin disassembly and assembly in the early embryo and in somatic cells.
Said Sif - One of the best experts on this subject based on the ideXlab platform.
-
the protein arginine methyltransferase prmt5 is required for myogenesis because it facilitates atp dependent Chromatin Remodeling
Molecular and Cellular Biology, 2007Co-Authors: Caroline S Dacwag, Said Sif, Yasuyuki Ohkawa, Sharmistha Pal, Anthony N ImbalzanoAbstract:Skeletal muscle differentiation requires the coordinated activity of transcription factors, histone modifying enzymes, and ATP-dependent Chromatin Remodeling enzymes. The type II protein arginine methyltransferase Prmt5 symmetrically dimethylates histones H3 and H4 and numerous nonChromatin proteins, and prior work has implicated Prmt5 in transcriptional repression. Here we demonstrate that MyoD-induced muscle differentiation requires Prmt5. One of the first genes activated during differentiation encodes the myogenic regulator myogenin. Prmt5 and dimethylated H3R8 (histone 3 arginine 8) are localized at the myogenin promoter in differentiating cells. Modification of H3R8 required Prmt5, and reduction of Prmt5 resulted in the abrogation of promoter binding by the Brg1 ATPase-associated with the SWI/SNF Chromatin Remodeling enzymes and all subsequent events associated with gene activation, including increases in Chromatin accessibility and stable binding by MyoD. Prmt5 and dimethylated H3R8 were also associated with the myogenin promoter in activated satellite cells isolated from muscle tissue, further demonstrating the physiological relevance of these observations. The data indicate that Prmt5 facilitates myogenesis because it is required for Brg1-dependent Chromatin Remodeling and gene activation at a locus essential for differentiation. We therefore conclude that a histone modifying enzyme is necessary to permit an ATP-dependent Chromatin Remodeling enzyme to function. Gene expression is a highly regulated process that frequently requires coordinated function between transcription factors and Chromatin Remodeling enzymes. These enzymes are divided into two classes: ATP-dependent remodelers that hydrolyze ATP and alter nucleosome structure and histone modifiers that covalently modify specific histone residues posttranslationally. The activation of skeletal muscle differentiation is regulated by members of the basic helix-loop-helix family of tissue-specific transcription factors, including MyoD, Myf5, Mrf4, and myogenin, as well as by members of the Mef2 family of transcriptional regulators, which act cooperatively with basic helix-loop-helix proteins (8, 34, 43). Numerous Chromatin Remodeling enzymes have been shown to both positively and negatively affect myogenic gene expression. These include histone acetyl transferases; types I, II; and III histone deacetylases; histone lysine methyltransferases; and members of the SWI/SNF family of ATP-dependent Remodeling enzymes (17, 47, 50). The relationships between the different classes of Chromatin Remodeling enzymes during myogenesis have been largely unexplored. The protein arginine methyltransferases (PRMTs) are an additional class of enzymes that can be linked to histone modification and gene regulation during skeletal muscle differentiation. This family has 9 members (Prmt1 to Prmt9), six of
-
the protein arginine methyltransferase prmt5 is required for myogenesis because it facilitates atp dependent Chromatin Remodeling
Molecular and Cellular Biology, 2007Co-Authors: Caroline S Dacwag, Said Sif, Yasuyuki Ohkawa, Sharmistha Pal, Anthony N ImbalzanoAbstract:Skeletal muscle differentiation requires the coordinated activity of transcription factors, histone modifying enzymes, and ATP-dependent Chromatin Remodeling enzymes. The type II protein arginine methyltransferase Prmt5 symmetrically dimethylates histones H3 and H4 and numerous nonChromatin proteins, and prior work has implicated Prmt5 in transcriptional repression. Here we demonstrate that MyoD-induced muscle differentiation requires Prmt5. One of the first genes activated during differentiation encodes the myogenic regulator myogenin. Prmt5 and dimethylated H3R8 (histone 3 arginine 8) are localized at the myogenin promoter in differentiating cells. Modification of H3R8 required Prmt5, and reduction of Prmt5 resulted in the abrogation of promoter binding by the Brg1 ATPase-associated with the SWI/SNF Chromatin Remodeling enzymes and all subsequent events associated with gene activation, including increases in Chromatin accessibility and stable binding by MyoD. Prmt5 and dimethylated H3R8 were also associated with the myogenin promoter in activated satellite cells isolated from muscle tissue, further demonstrating the physiological relevance of these observations. The data indicate that Prmt5 facilitates myogenesis because it is required for Brg1-dependent Chromatin Remodeling and gene activation at a locus essential for differentiation. We therefore conclude that a histone modifying enzyme is necessary to permit an ATP-dependent Chromatin Remodeling enzyme to function.
-
ikaros dna binding proteins direct formation of Chromatin Remodeling complexes in lymphocytes
Immunity, 1999Co-Authors: John Kim, Said Sif, B Jones, Audrey F Jackson, Joseph Koipally, Elizabeth J Heller, Susan Winandy, Alain Viel, Alan Sawyer, Toru IkedaAbstract:The Ikaros gene family encodes zinc finger DNA-binding proteins essential for lineage determination and control of proliferation in the lymphoid system. Here, we report that, in the nucleus of a T cell, a major fraction of Ikaros and Aiolos proteins associate with the DNA-dependent ATPase Mi-2 and histone deacetylases, in a 2 MD complex. This Ikaros-NURD complex is active in Chromatin Remodeling and histone deacetylation. Upon T cell activation, Ikaros recruits Mi-2/HDAC to regions of heteroChromatin. These studies reveal that Ikaros proteins are capable of targeting Chromatin Remodeling and deacetylation complexes in vivo. We propose that the restructuring of Chromatin is a key aspect of Ikaros function in lymphocyte differentiation.
Caroline S Dacwag - One of the best experts on this subject based on the ideXlab platform.
-
the protein arginine methyltransferase prmt5 is required for myogenesis because it facilitates atp dependent Chromatin Remodeling
Molecular and Cellular Biology, 2007Co-Authors: Caroline S Dacwag, Said Sif, Yasuyuki Ohkawa, Sharmistha Pal, Anthony N ImbalzanoAbstract:Skeletal muscle differentiation requires the coordinated activity of transcription factors, histone modifying enzymes, and ATP-dependent Chromatin Remodeling enzymes. The type II protein arginine methyltransferase Prmt5 symmetrically dimethylates histones H3 and H4 and numerous nonChromatin proteins, and prior work has implicated Prmt5 in transcriptional repression. Here we demonstrate that MyoD-induced muscle differentiation requires Prmt5. One of the first genes activated during differentiation encodes the myogenic regulator myogenin. Prmt5 and dimethylated H3R8 (histone 3 arginine 8) are localized at the myogenin promoter in differentiating cells. Modification of H3R8 required Prmt5, and reduction of Prmt5 resulted in the abrogation of promoter binding by the Brg1 ATPase-associated with the SWI/SNF Chromatin Remodeling enzymes and all subsequent events associated with gene activation, including increases in Chromatin accessibility and stable binding by MyoD. Prmt5 and dimethylated H3R8 were also associated with the myogenin promoter in activated satellite cells isolated from muscle tissue, further demonstrating the physiological relevance of these observations. The data indicate that Prmt5 facilitates myogenesis because it is required for Brg1-dependent Chromatin Remodeling and gene activation at a locus essential for differentiation. We therefore conclude that a histone modifying enzyme is necessary to permit an ATP-dependent Chromatin Remodeling enzyme to function. Gene expression is a highly regulated process that frequently requires coordinated function between transcription factors and Chromatin Remodeling enzymes. These enzymes are divided into two classes: ATP-dependent remodelers that hydrolyze ATP and alter nucleosome structure and histone modifiers that covalently modify specific histone residues posttranslationally. The activation of skeletal muscle differentiation is regulated by members of the basic helix-loop-helix family of tissue-specific transcription factors, including MyoD, Myf5, Mrf4, and myogenin, as well as by members of the Mef2 family of transcriptional regulators, which act cooperatively with basic helix-loop-helix proteins (8, 34, 43). Numerous Chromatin Remodeling enzymes have been shown to both positively and negatively affect myogenic gene expression. These include histone acetyl transferases; types I, II; and III histone deacetylases; histone lysine methyltransferases; and members of the SWI/SNF family of ATP-dependent Remodeling enzymes (17, 47, 50). The relationships between the different classes of Chromatin Remodeling enzymes during myogenesis have been largely unexplored. The protein arginine methyltransferases (PRMTs) are an additional class of enzymes that can be linked to histone modification and gene regulation during skeletal muscle differentiation. This family has 9 members (Prmt1 to Prmt9), six of
-
the protein arginine methyltransferase prmt5 is required for myogenesis because it facilitates atp dependent Chromatin Remodeling
Molecular and Cellular Biology, 2007Co-Authors: Caroline S Dacwag, Said Sif, Yasuyuki Ohkawa, Sharmistha Pal, Anthony N ImbalzanoAbstract:Skeletal muscle differentiation requires the coordinated activity of transcription factors, histone modifying enzymes, and ATP-dependent Chromatin Remodeling enzymes. The type II protein arginine methyltransferase Prmt5 symmetrically dimethylates histones H3 and H4 and numerous nonChromatin proteins, and prior work has implicated Prmt5 in transcriptional repression. Here we demonstrate that MyoD-induced muscle differentiation requires Prmt5. One of the first genes activated during differentiation encodes the myogenic regulator myogenin. Prmt5 and dimethylated H3R8 (histone 3 arginine 8) are localized at the myogenin promoter in differentiating cells. Modification of H3R8 required Prmt5, and reduction of Prmt5 resulted in the abrogation of promoter binding by the Brg1 ATPase-associated with the SWI/SNF Chromatin Remodeling enzymes and all subsequent events associated with gene activation, including increases in Chromatin accessibility and stable binding by MyoD. Prmt5 and dimethylated H3R8 were also associated with the myogenin promoter in activated satellite cells isolated from muscle tissue, further demonstrating the physiological relevance of these observations. The data indicate that Prmt5 facilitates myogenesis because it is required for Brg1-dependent Chromatin Remodeling and gene activation at a locus essential for differentiation. We therefore conclude that a histone modifying enzyme is necessary to permit an ATP-dependent Chromatin Remodeling enzyme to function.
John L Pulice - One of the best experts on this subject based on the ideXlab platform.
-
binding of tmprss2 erg to baf Chromatin Remodeling complexes mediates prostate oncogenesis
Molecular Cell, 2018Co-Authors: Gabriel J Sandoval, John L Pulice, Hubert Pakula, Monica Schenone, David Y Takeda, Gaylor BoulayAbstract:Summary Chromosomal rearrangements resulting in the fusion of TMPRSS2, an androgen-regulated gene, and the ETS family transcription factor ERG occur in over half of prostate cancers. However, the mechanism by which ERG promotes oncogenic gene expression and proliferation remains incompletely understood. Here, we identify a binding interaction between ERG and the mammalian SWI/SNF (BAF) ATP-dependent Chromatin Remodeling complex, which is conserved among other oncogenic ETS factors, including ETV1, ETV4, and ETV5. We find that ERG drives genome-wide retargeting of BAF complexes in a manner dependent on binding of ERG to the ETS DNA motif. Moreover, ERG requires intact BAF complexes for Chromatin occupancy and BAF complex ATPase activity for target gene regulation. In a prostate organoid model, BAF complexes are required for ERG-mediated basal-to-luminal transition, a hallmark of ERG activity in prostate cancer. These observations suggest a fundamental interdependence between ETS transcription factors and BAF Chromatin Remodeling complexes in cancer.
-
composition and function of mammalian swi snf Chromatin Remodeling complexes in human disease
Cold Spring Harbor Symposia on Quantitative Biology, 2016Co-Authors: John L Pulice, Cigall KadochAbstract:Mammalian SWI/SNF (BAF) Chromatin Remodeling complexes play critical roles in maintaining Chromatin architecture and gene expression. Genomic sequencing efforts over the past several years have unveiled a major role for these complexes in the development of human cancer as well as neurologic disease, prompting the need to interrogate underlying mechanisms and to develop new methods to comprehensively understand mSWI/SNF complex function. Here we discuss the emerging insights from genetic, biochemical, and functional genomic studies in the field and suggest approaches toward further basic investigations, as well as therapeutic targeting of Chromatin Remodeling machinery.