The WSTF-SNF2h Chromatin Remodeling Complex Interacts with Several Nuclear Proteins in Transcription

Cavellán, Erica; Asp, Patrik; Percipalle, Piergiorgio; Farrants, Ann Kristin Östlund

doi:10.1074/jbc.m600233200

Cited by 139 publications

(135 citation statements)

References 59 publications

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“…Subfamily III of BRDs contains the transcriptional regulator bromodomain containing 8B (BRD8B) [55], the HAT enzymes CREB binding protein (CREBBP) and E1A binding protein p300 (EP300) [56], the C-terminal domain of the chromatin remodelling factors WD repeat domain 9 (WDR9 domain 2) [57], the bromodomain adjacent to zinc finger domain 1B (BAZ1B) [25], the C-terminal domain of the JAK/STAT pathway related bromodomain-containing protein disrupted in leukemia (BRWD3 domain 2) [58] and the C-terminal domain of the insulin signalling related pleckstrin homology domain interacting protein (PHIP domain 2) [59]. Following the idea of targeting enzymatic HAT activity to specific sites via recognition of acetyl-lysine motifs, the BRDs of CREBBP and EP300 have been extensively studied in the context of histone binding.…”

Section: Bromodomain Substratesmentioning

confidence: 99%

The bromodomain interaction module

2012

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a b s t r a c t e-N-acetylation of lysine residues (K ac ) is one of the most abundant post-translation modifications (PTMs) in the human proteome. In the nucleus, acetylation of histones has been linked to transcriptional activation of genes but the functional consequences of most acetylation events and proteins recruited to these sites remains largely unknown. Bromodomains (BRDs) are small helical interaction modules that specifically recognize acetylation sites in proteins. BRDs have recently emerged as interesting targets for the development of specific protein interaction inhibitors, enabling a novel exiting strategy for the development of new therapies. This review provides an overview over sequence requirements of BRDs, known substrates and the structural mechanisms of specific K ac recognition.

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Section: Bromodomain Substratesmentioning

confidence: 99%

The bromodomain interaction module

2012

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“…One possibility is that additional modification of DEK might determine its target specificity (Kappes et al, 2004;Scoumanne and Chen, 2007). Another, but not exclusive, idea is that additional cooperation with other transcriptional factors or nucleosome/chromatin assembly factors may mark specific DEK binding or work cooperatively and induce characteristic transcriptional changes, as DEK has been shown to interact with several epigenetic modifiers (Hollenbach et al, 2002;Cleary et al, 2005;Cavella´n et al, 2006). These hypotheses may also explain why broadly expressed DEK is associated with the tumor-initiating cells, a supposedly rare tumor subpopulation.…”

Section: Molecular Classification Of Pulmonary Endocrine Tumorsmentioning

confidence: 99%

DEK oncoprotein regulates transcriptional modifiers and sustains tumor initiation activity in high-grade neuroendocrine carcinoma of the lung

Shibata¹,

Kokubu²,

Miyamoto³

et al. 2010

Oncogene

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Lung cancer shows diverse histological subtypes. Largecell neuroendocrine cell carcinoma and small-cell lung carcinoma show similar histological features and clinical behaviors, and can be classified as high-grade neuroendocrine carcinoma (HGNEC) of the lung. Here we elucidated the molecular classification of pulmonary endocrine tumors by copy-number profiling. We compared alterations of copy number with the clinical outcome of HGNEC and identified a chromosomal gain of the DEK oncogene locus (6p22.3) that was significantly associated with poor prognosis. We further confirmed that DEK overexpression was associated with poor prognosis in a larger set of HGNEC. Downregulation of DEK by small hairpin RNA led to a marked reduction of in vitro colony formation, in vivo tumorigenicity and chemo-resistance, and was associated with loss of lung cancer stem cell markers. Gene expression profiling revealed that DEK downregulation was associated with altered expression of transcriptional regulators, which specifically include known targets of interchromosomal translocations in hematopoietic tumors, and knockdown of these epigenetic modifiers affected colony formation activity. Our study showed that DEK overexpression, partly through an increase in its gene dose, mediates the activity of global transcriptional regulators and is associated with tumor initiation activity and poor prognosis in HGNEC.

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“…3B), also co-localized with Pol I in the nucleoli (30). SNF2h corresponds to the human imitation switch (ISWI) enzyme that exhibits ATP-dependent chromatin remodeling function in the B-WICH complex (34).…”

Section: Sirt7 Interacts With Pol I Ubf and B-wich Components In Thementioning

confidence: 99%

“…WSTF (gene name BAZ1B), SNF2h (gene name SMARCA5), Mybbp1a, SAP155 (gene name SF3B1), RH-II/GU (gene name DDX21), and myosin I (gene name MYO1C) are part of the B-WICH complex (34). B-WICH is an ATP-dependent chromatin remodeling complex that has been shown to associate with the Pol I machinery, facilitating rDNA transcription (30).…”

Section: Sirt7 Interacts With Pol I Ubf and B-wich Components In Thementioning

confidence: 99%

Functional Proteomics Establishes the Interaction of SIRT7 with Chromatin Remodeling Complexes and Expands Its Role in Regulation of RNA Polymerase I Transcription

Tsai¹,

Greco²,

Boonmee

et al. 2012

Molecular & Cellular Proteomics

121

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Among mammalian sirtuins, SIRT7 is the only enzyme residing in nucleoli where ribosomal DNA is transcribed. Recent reports established that SIRT7 associates with RNA Pol I machinery and is required for rDNA transcription. Although defined by its homology to the yeast histone deacetylase Sir2, current knowledge suggests that SIRT7 itself has little to no deacetylase activity. Because only two SIRT7 interactions have been thus far described: RNA Pol I and upstream binding factor, identification of proteins and complexes associating with SIRT7 is critical to understanding its functions. Here, we present the first characterization of SIRT7 interaction networks. We have systematically investigated protein interactions of three EGFP-tagged SIRT7 constructs: wild type, a point mutation affecting rDNA transcription, and a deletion mutant lacking the predicted coiled-coil domain. A combinatorial proteomics and bioinformatics approach was used to integrate gene ontology classifications, functional protein networks, and normalized abundances of proteins coisolated with SIRT7. The resulting refined proteomic data set confirmed SIRT7 interactions with RNA Pol I and upstream binding factor and highlighted association with factors involved in RNA Pol I-and II-dependent transcriptional processes and several nucleolus-localized chromatin remodeling complexes. Particularly enriched were members of the B-WICH complex, such as Mybbp1a, WSTF, and SNF2h. Prominent interactions were validated by a selected reaction monitoring-like approach using metabolic labeling with stable isotopes, confocal microscopy, reciprocal immunoaffinity precipitation, and co-isolation with endogenous SIRT7. To extend the current knowledge of mechanisms involved in SIRT7-dependent regulation of rDNA transcription, we showed that small interfering RNA-mediated SIRT7 knockdown leads to reduced levels of RNA Pol I protein, but not messenger RNA, which was confirmed in diverse cell types. The correlation between histone acetylation status and transcriptional regulation is well established in that hyperacetylation is commonly associated with transcriptional activation, whereas hypoacetylation is associated with transcriptional repression (1-3). In eukaryotes, Sir2-like proteins form a family of enzymes known as sirtuins (4). Distinct from class I and II histone deacetylases (HDACs), which facilitate hydrolysis of acetyl-lysine as a bimolecular reaction (5), sirtuins consume an equimolar amount of nicotinamide adenine dinucleotide (NAD ϩ ) for each hydrolysis reaction and generate nicotinamide, O-acetyl ADP-ribose, and deacetylated substrate as end products (4). Based on homology of the sirtuin core domain, there are seven sirtuins (SIRT1-7) in human cells with functions not limited to histone deacetylation, because many additional cellular proteins have been identified as substrates (4, 6). In addition, the localizations of human sirtuins are distributed across multiple organelles including nucleolus, nucleus, cytoplasm, and mitochondria (7).Systematic monitorin...

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The WSTF-SNF2h Chromatin Remodeling Complex Interacts with Several Nuclear Proteins in Transcription

Cited by 139 publications

References 59 publications

The bromodomain interaction module

The bromodomain interaction module

DEK oncoprotein regulates transcriptional modifiers and sustains tumor initiation activity in high-grade neuroendocrine carcinoma of the lung

Functional Proteomics Establishes the Interaction of SIRT7 with Chromatin Remodeling Complexes and Expands Its Role in Regulation of RNA Polymerase I Transcription

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