The adenovirus E1A oncoprotein recruits the cellular TRRAP/GCN5 histone acetyltransferase complex

Lang, Stanley; Hearing, Patrick

doi:10.1038/sj.onc.1206376

Cited by 77 publications

(79 citation statements)

References 29 publications

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“…These include c-Myc, p53, E2F1, E2F4, E1A, ERa, ERb, VDR, PPARg, LXR, FXR, b-catenin, Skp1 and BRCA1 Lang et al, 2001;Park et al, 2001;Ard et al, 2002;Yanagisawa et al, 2002;Lang and Hearing, 2003;Unno et al, 2005;Cheng et al, 2006;Oishi et al, 2006;Sierra et al, 2006;Finkbeiner and Herceg, unpublished results). Interestingly, the TRRAP domains that interact with diverse partners are not overlapping and it can be speculated that TRRAP may serve not only as a scaffold for HAT complexes but also as a platform for recruitment of different regulatory factors and complexes to chromatin.…”

Section: Cellular Pools Of Trrapmentioning

confidence: 91%

“…The evidence that simultaneous enrichment of TRRAP, transcription factors and HATs at chromatin is associated with promoter-specific chromatin hyperacetylation Bouchard et al, 2001;Frank et al, 2001;Herceg et al, 2003;Li et al, 2004;Taubert et al, 2004) led to the suggestion that TRRAP functions to recruit HAT complexes to transcription factors bound to their target promoters in chromatin. TRRAP was found as a target of the adenovirus E1A oncoprotein and to be important for oncogenic transformation mediated by viral oncoproteins Deleu et al, 2001;Lang et al, 2001;Lang and Hearing, 2003). We have recently shown that Trrap is involved in the repair of DNA double-strand breaks (DSBs) , indicating that the function of TRRAP and TRRAP-mediated histone acetylation is not limited to transcriptional control, but likely extents to all chromatin-based processes that use DNA as a template.…”

Section: Introductionmentioning

confidence: 99%

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Orchestration of chromatin-based processes: mind the TRRAP

et al. 2007

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Chromatin modifications at core histones including acetylation, methylation, phosphorylation and ubiquitination play an important role in diverse biological processes. Acetylation of specific lysine residues within the N terminus tails of core histones is arguably the most studied histone modification; however, its precise roles in different cellular processes and how it is disrupted in human diseases remain poorly understood. In the last decade, a number of histone acetyltransferases (HATs) enzymes responsible for histone acetylation, has been identified and functional studies have begun to unravel their biological functions. The activity of many HATs is dependent on HAT complexes, the multiprotein assemblies that contain one HAT catalytic subunit, adapter proteins, several other molecules of unknown function and a large protein called TRansformation/tRanscription domain-Associated Protein (TRRAP). As a common component of many HAT complexes, TRRAP appears to be responsible for the recruitment of these complexes to chromatin during transcription, replication and DNA repair. Recent studies have shed new light on the role of TRRAP in HAT complexes as well as mechanisms by which it mediates diverse cellular processes. Thus, TRRAP appears to be responsible for a concerted and context-dependent recruitment of HATs and coordination of distinct chromatin-based processes, suggesting that its deregulation may contribute to diseases. In this review, we summarize recent developments in our understanding of the function of TRRAP and TRRAP-containing HAT complexes in normal cellular processes and speculate on the mechanism underlying abnormal events that may lead to human diseases such as cancer.

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Section: Cellular Pools Of Trrapmentioning

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Orchestration of chromatin-based processes: mind the TRRAP

et al. 2007

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“…Like Tip60 itself, the NuA4 subunits BAF53a, TRRAP and p400 have been implicated in c-Myc oncogene-mediated cellular transformation (Fuchs et al, 2001;Nikiforov et al, 2002;Park et al, 2002). Both TRRAP and p400 are also targeted by the adenoviral E1A oncoprotein and are essential for E1A-mediated cellular transformation (Fuchs et al, 2001;Lang and Hearing, 2003). Although the adenovirus is not associated with human malignancy, this evidence implies that TRRAP and p400 play key roles in cellular regulation and can be subverted to promote oncogenesis.…”

Section: Tip60-associated Proteins and Their Links To Cancermentioning

confidence: 99%

The MYST family of histone acetyltransferases and their intimate links to cancer

2007

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The histone acetyltransferases (HATs) of the MYST family are highly conserved in eukaryotes and carry out a significant proportion of all nuclear acetylation. These enzymes function exclusively in multisubunit protein complexes whose composition is also evolutionarily conserved. MYST HATs are involved in a number of key nuclear processes and play critical roles in genespecific transcription regulation, DNA damage response and repair, as well as DNA replication. This suggests that anomalous activity of these HATs or their associated complexes can easily lead to severe cellular malfunction, resulting in cell death or uncontrolled growth and malignancy. Indeed, the MYST family HATs have been implicated in several forms of human cancer. This review summarizes the current understanding of these enzymes and their normal function, as well as their established and putative links to oncogenesis.

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“…There are many reports of the histone acetyltransferases such as PCAF, p300/CBP and GCN5 acting as co-activators (Benkirane et al, 1998;Vassilev et al, 1998;Hamamori et al, 1999;Jiang et al, 1999;Masumi et al, 1999;Schiltz et al, 1999;Harrod et al, 2000;Lau et al, 2000a, b;Li et al, 2000;Trievel et al, 2000;Yamauchi et al, 2000;Vo and Goodman, 2001;Lang and Hearing, 2003;Patel et al, 2004). A number of transcriptional factors associate with p300/CBP, originally known as the global co-activator, and with PCAF and GCN5.…”

Section: Introductionmentioning

confidence: 99%

Nucleolin is involved in interferon regulatory factor-2-dependent transcriptional activation

et al. 2006

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We have previously shown that Interferon regulatory factor‐2 (IRF‐2) is acetylated in a cell growth‐dependent manner, which enables it to contribute to the transcription of cell growth‐regulated promoters. To clarify the function of the acetylation of IRF‐2, we investigated the proteins that associate with acetylated IRF‐2. Transfection of p300/CBP‐associated factor (PCAF) enhanced acetylation of IRF‐2 in 293T cells. In cells transfected with both IRF‐2 and PCAF, IRF‐2 associated with endogenous nucleolin, in contrast, little association was observed when IRF‐2 was transfected with a PCAF HAT deletion mutant. In a pull‐down experiment using stable transfectants, acetylation defective mutant IRF‐2 (IRF‐2K75R) recruited nucleolin to much lower degree than that of wild type IRF‐2, suggesting that nucleolin preferentially associates with acetylated IRF‐2. Confocal analysis indicated that IRF‐2 colocalized with nucleolin in the perinucleolar region. Nucleolin in the presence of PCAF enhanced IRF‐2‐dependent H4 promoter activity in NIH3T3 cells. Affinity DNA binding analysis with H4 promoter DNA indicated that nucleolin associated with IRF‐2 in growing NIH3T3 cells, but not in growth‐arrested counterparts. We conclude that nucleolin is recruited to acetylated IRF‐2, contributing to gene regulation crucial for the control of cell growth.

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The adenovirus E1A oncoprotein recruits the cellular TRRAP/GCN5 histone acetyltransferase complex

Cited by 77 publications

References 29 publications

Orchestration of chromatin-based processes: mind the TRRAP

Orchestration of chromatin-based processes: mind the TRRAP

The MYST family of histone acetyltransferases and their intimate links to cancer

Nucleolin is involved in interferon regulatory factor-2-dependent transcriptional activation

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