{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bonham CA"],"funding":["Natural Sciences and Engineering Research Council of Canada","Cold Spring Harbor Laboratory","National Institutes of Health","ShanghaiTech University","Don Monti Memorial Research Foundation"],"pagination":["104582"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10148153"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["299(5)"],"pubmed_abstract":["The ability to define functional interactions between enzymes and their substrates is crucial for understanding biological control mechanisms; however, such methods face challenges in the transient nature and low stoichiometry of enzyme-substrate interactions. Now, we have developed an optimized strategy that couples substrate-trapping mutagenesis to proximity-labeling mass spectrometry for quantitative analysis of protein complexes involving the protein tyrosine phosphatase PTP1B. This methodology represents a significant shift from classical schemes; it is capable of being performed at near-endogenous expression levels and increasing stoichiometry of target enrichment without a requirement for stimulation of supraphysiological tyrosine phosphorylation levels or maintenance of substrate c"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Coupling substrate-trapping with proximity-labeling to identify protein tyrosine phosphatase PTP1B signaling networks."],"pmcid":["PMC10148153"],"funding_grant_id":["CA53840","CA45508"],"pubmed_authors":["Singh RK","Mandati V","Tonks NK","Pappin DJ","Bonham CA"],"additional_accession":[]},"is_claimable":false,"name":"Coupling substrate-trapping with proximity-labeling to identify protein tyrosine phosphatase PTP1B signaling networks.","description":"The ability to define functional interactions between enzymes and their substrates is crucial for understanding biological control mechanisms; however, such methods face challenges in the transient nature and low stoichiometry of enzyme-substrate interactions. Now, we have developed an optimized strategy that couples substrate-trapping mutagenesis to proximity-labeling mass spectrometry for quantitative analysis of protein complexes involving the protein tyrosine phosphatase PTP1B. This methodology represents a significant shift from classical schemes; it is capable of being performed at near-endogenous expression levels and increasing stoichiometry of target enrichment without a requirement for stimulation of supraphysiological tyrosine phosphorylation levels or maintenance of substrate c","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Mar","modification":"2025-04-21T17:24:23.273Z","creation":"2025-04-05T16:40:40.315Z"},"accession":"S-EPMC10148153","cross_references":{"pubmed":["36871762"],"doi":["10.1016/j.jbc.2023.104582"]}}