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PABPC1 stress granule interactome identified by BioID

ABSTRACT: Identification of Stress Granule interacting proteins by BioID (Roux et al., 2012) using PABPC1-BirA(R118G)-GFP construct

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Triana Amen

LAB HEAD: Daniel Kaganovich

PROVIDER: PXD025334 | Pride | 2022-02-17

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	SG.xml	Xml
	StressGranules.xlsx	Xlsx
	checksum.txt	Txt

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Publications

Stress granules inhibit fatty acid oxidation by modulating mitochondrial permeability.

Amen Triana T Kaganovich Daniel D

Cell reports 20210601 11

The formation of stress granules (SGs) is an essential aspect of the cellular response to many kinds of stress, but its adaptive role is far from clear. SG dysfunction is implicated in aging-onset neurodegenerative diseases, prompting interest in their physiological function. Here, we report that during starvation stress, SGs interact with mitochondria and regulate metabolic remodeling. We show that SG formation leads to a downregulation of fatty acid β-oxidation (FAO) through the modulation of ...[more]

PMID: 34133922

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Fasnall induces atpically transient Stress Granules

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

Project description: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.

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Proteome of arsenite in P. pseudoalcaligenes CECT 5344

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Remodeling of Ago2-mRNA interactions upon cellular stress reflects miRNA complementarity and correlates with altered translation rates (part 4)

Project description:When adapting to environmental stress, cells attenuate and reprogram their translational output. In part, these altered translation profiles are established through changes in the interactions between RNA-binding proteins and mRNAs. The Ago2/microRNA machinery has been shown to participate in stress-induced translational upregulation of a particular mRNA, CAT-1; however, a detailed, transcriptome-wide understanding of the involvement of Ago2 in the process has been lacking. Here, we profiled the overall changes in Ago2-mRNA interactions upon arsenite stress by CLIP-seq. Ago2 displayed a significant remodeling of its transcript occupancy, with the majority of 3` UTR and CDS sites exhibiting stronger interaction. Interestingly, target sites that were destined for release from Ago2 upon stress were depleted in miRNA complementarity signatures, suggesting an alternative mode of interaction. To compare the changes in Ago2 binding patterns across transcripts with changes in their translational states, we measured mRNA profiles on ribosome/polysome gradients by RNA-seq. Increased Ago2 occupancy correlated with stronger repression of translation for those mRNAs, as evidenced by a shift toward lighter gradient fractions upon stress, while release of Ago2 was associated with the limited number of transcripts that remained translated. Taken together, these data point to a role for Ago2 and the mammalian microRNAs in mediating the translational component of the stress response. In this sub-series, RNAseq data from sucrose gradient fractions with arsenite treatment are presented.

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