Dataset Information

Proximity-biotinylation (BioID) to dissect cytoplasmic p53 signaling networks under nutrient stress

ABSTRACT: p53 signaling is a major response mechanism to cellular stresses through cytoplasmic or nuclear action. While p53 protein levels have been shown to increase upon nutrient stresses such as starvation, the exact signaling cascade in this context remains elusive. Here, we use proximity biotinylation (BioID), to derive the cytoplasmic p53 interaction network as immediate early starvation response.

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hepatocyte, Cell Culture

SUBMITTER: Markus Galhuber

LAB HEAD: Andreas Prokesch

PROVIDER: PXD027734 | Pride | 2022-06-09

REPOSITORIES: Pride

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Publications

Complementary omics strategies to dissect p53 signaling networks under nutrient stress.

Galhuber Markus M Michenthaler Helene H Heininger Christoph C Reinisch Isabel I Nössing Christoph C Krstic Jelena J Kupper Nadja N Moyschewitz Elisabeth E Auer Martina M Heitzer Ellen E Ulz Peter P Birner-Gruenberger Ruth R Liesinger Laura L Lenihan-Geels Georgia Ngawai GN Oster Moritz M Spreitzer Emil E Zenezini Chiozzi Riccardo R Schulz Tim J TJ Schupp Michael M Madl Tobias T Heck Albert J R AJR Prokesch Andreas A

Cellular and molecular life sciences : CMLS 20220530 6

Signaling trough p53is a major cellular stress response mechanism and increases upon nutrient stresses such as starvation. Here, we show in a human hepatoma cell line that starvation leads to robust nuclear p53 stabilization. Using BioID, we determine the cytoplasmic p53 interaction network within the immediate-early starvation response and show that p53 is dissociated from several metabolic enzymes and the kinase PAK2 for which direct binding with the p53 DNA-binding domain was confirmed with N ...[more]

PMID: 35635656

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Project description:Here we exploit the essential process of X-chromosome dosage compensation to elucidate basic mechanisms that control the assembly, genome-wide binding, and function of gene regulatory complexes that act over large chromosomal territories. We demonstrate that a subunit of C. elegans MLL/COMPASS, a gene-activation complex, acts within the dosage compensation complex (DCC), a condensin complex, to target the DCC to both X chromosomes of hermaphrodites and thereby reduce chromosome-wide gene expression. The DCC binds to two categories of sites on X: rex sites that recruit the DCC in an autonomous, sequence- dependent manner, and dox sites that reside primarily in promoters of expressed genes and bind the DCC robustly only when attached to X. We find that DCC mutants that abolish rex-site binding do not eliminate dox-site binding, but instead reduce it to the level observed at autosomal binding sites in wild-type animals. Changes in DCC binding to these non-rex sites occur throughout development and correlate with transcriptional activity of adjacent genes. Moreover, autosomal DCC binding is enhanced by rex-site binding in cis in X-autosome fusion chromosomes. Thus, dox and autosomal sites exhibit similar binding properties. Our data support a model for DCC binding in which low-level DCC binding at dox and autosomal sites is dictated by intrinsic properties correlated with high transcriptional activity. Sex-specific DCC recruitment to rex sites then greatly elevates DCC binding to dox sites in cis, which lack intrinsically high DCC affinity on their own. We also show here that the C. elegans DCC achieves dosage compensation through its effects on transcription. ChIP-chip experiments using antibodies against DPY-27, SDC-3, DPY-30, DPY-26, MIX-1, SMC-4, ASH-2 in wild-type embryos. ChIP-chip experiments using antibodies against SDC-3, DPY-27, DPY-30, ASH-2, and IgG in different DCC mutants. ChIP-chip experiments using antibodies against RNA Pol II (hypophosphorylated and S2 and S5) in wild type and sdc-2 partial loss of function mutants.

Dataset Information

Proximity-biotinylation (BioID) to dissect cytoplasmic p53 signaling networks under nutrient stress

Publications

Complementary omics strategies to dissect p53 signaling networks under nutrient stress.

Similar Datasets

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