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Acetylation site mapping on TULP3

ABSTRACT: Fig. 2B: Semi-quantitative acetylation level on TULP3 in the presence of either empty pcDNA 3.1(+), Myc-p300, FLAG-PCAF or FLAG-GCN5 following immunoprecipitation.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Olivier Julien Basil Hubbard

PROVIDER: MSV000086358 | MassIVE | Thu Oct 22 10:29:00 BST 2020

REPOSITORIES: MassIVE

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Publications

A conserved acetylation switch enables pharmacological control of tubby-like protein stability.

Kerek Evan M EM Yoon Kevin H KH Luo Shu Y SY Chen Jerry J Valencia Robert R Julien Olivier O Waskiewicz Andrew J AJ Hubbard Basil P BP

The Journal of biological chemistry 20201123

Tubby-like proteins (TULPs) are characterized by a conserved C-terminal domain that binds phosphoinositides. Collectively, mammalian TULP1-4 proteins play essential roles in intracellular transport, cell differentiation, signaling, and motility. Yet, little is known about how the function of these proteins is regulated in cells. Here, we present the protein-protein interaction network of TULP3, a protein that is responsible for the trafficking of G-protein-coupled receptors to cilia and whose ab ...[more]

PMID: 33187986

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Histone exchange and histone H4 acetylation in wild-type and SET2 deletion yeast strains

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Combination Targeting of the Bromodomain and Acetyltransferase Active Site of p300/CBP [RNA-seq]

Project description:p300 and CBP are highly related histone acetyltransferase (HAT) enzymes that regulate gene expression, and their dysregulation has been linked to cancer and other diseases. p300/CBP is composed of a number of domains including a HAT domain which is inhibited by the small molecule A-485 and an acetyl-lysine binding bromodomain which was recently found to be selectively antagonized by the small molecule I-CBP112. Here we show that the combination of I-CBP112 and A-485 can synergize to inhibit prostate cancer cell proliferation. We find that the combination confers a dramatic reduction in p300 chromatin occupancy compared to the individual effects of blocking either domain alone. Accompanying this loss of p300 on chromatin, combination treatment predominantly leads to the reduction of specific mRNAs including androgen-dependent and pro-oncogenic prostate genes such as KLK3 (PSA) and c-Myc. Consistent with p300 chromatin binding directly affecting gene expression, mRNAs that are significantly reduced by combination treatment also exhibit a strong reduction in p300 chromatin occupancy at their gene promoters. The relatively few mRNAs that are up-regulated upon combination treatment show no correlation with p300 occupancy. These studies provide support for the pharmacologic advantage of concurrent targeting of two domains within one key epigenetic modification enzyme.

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RNA helicase DDX5-induced circPHF14 promotes gastric cancer cell progression

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