Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Systematic investigation of the correlation between protein modifications and distributions in the nucleus and the cytoplasm

ABSTRACT: We comprehensively investigate the differences of the nuclear-cytoplasmic distributions of the modified (phosphorylated and O-GlcNAcylated) and non-modified forms of proteins to dissect the correlation between the distributions and modifications of proteins.

INSTRUMENT(S): LTQ Orbitrap Elite

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

SUBMITTER: Ronghu Wu

PROVIDER: MSV000088883 | MassIVE | Mon Feb 21 16:24:00 GMT 2022

REPOSITORIES: MassIVE

ACCESS DATA

Json Xml

Similar Datasets

Spatial and temporal proteomics reveals distinct distribution and dynamics of O-GlcNAcylated proteins

Project description:Protein O-GlcNAcylation plays critical roles in many cellular events, and its dysregulation is related to multiple diseases. Integrating bioorthogonal chemistry and multiplexed proteomics, we systematically and site-specifically study the distributions and dynamics of protein O-GlcNAcylation in the nucleus and the cytoplasm of human cells. The results demonstrate that O-GlcNAcylated proteins with different functions have distinct distribution patterns, and the distributions vary site-specifically. Moreover, the dynamics of O-GlcNAcylated proteins and non-modified ones in these two compartments are comprehensively analyzed, respectively, and the half-lives of glycoproteins in different compartments are markedly different with the median half-life in the cytoplasm being about two times longer than that in the nucleus. Additionally, glycoproteins in the nucleus are more dramatically stabilized than those in the cytoplasm under the O-GlcNAcase inhibition. The comprehensive spatial and temporal analyses of protein O-GlcNAcylation provide valuable information and advance our understanding of this important modification.

2022-05-03 | MSV000089413 | MassIVE

Systematic investigation on the effect of O-GlcNAcylation on condensate formation under heat stress and recovery

Project description:O-GlcNAc is known to regulate the aggregation and condensate formation of several proteins, but how O-GlcNAc regulates protein solubilities globally has yet to be systematically investigated. Here, we employed a chemoproteomic workflow integrating selective enrichment and multiplex proteomics to quantify the solubilities of O-GlcNAcylated and non-modified proteins, as well as their role in RNA condensate formation. The solubilities were also quantified after heat stress and recovery to investigate the condensate formation during heat stress response. Surprisingly. we found O-GlcNAc leads to dramatic solubility decrease of the modified proteins, and the degree of solubility drop is related to the protein localization and functions. Site-specific analysis found the adjacent residues and secondary structures of the glycosites are pivotal for the effect of O-GlcNAc for solubility change, and the number of acidic residues is related to the different effect of O-GlcNAc in heat stress and recovery. Additionally, it was found that O-GlcNAc promotes the dissociation of RNA condensates during heat stress, while it enhances the formation of RNA condensates in the recovery phase. The glycosites that facilitate the dissociation or the formation of the RNA condensates are distinct, and the physiological properties of their surroundings residues are diverse. This work advances our understanding of the role of O-GlcNAc in regulating biomolecular condensates and will be a useful resource for future research in biomolecular condensates.

2023-08-18 | MSV000092690 | MassIVE