{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Singh JP"],"funding":["NINDS NIH HHS","NIGMS NIH HHS"],"pagination":["94"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8748766"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(1)"],"pubmed_abstract":["T-Cell Protein Tyrosine Phosphatase (TCPTP, PTPN2) is a non-receptor type protein tyrosine phosphatase that is ubiquitously expressed in human cells. TCPTP is a critical component of a variety of key signaling pathways that are directly associated with the formation of cancer and inflammation. Thus, understanding the molecular mechanism of TCPTP activation and regulation is essential for the development of TCPTP therapeutics. Under basal conditions, TCPTP is largely inactive, although how this is achieved is poorly understood. By combining biomolecular nuclear magnetic resonance spectroscopy, small-angle X-ray scattering, and chemical cross-linking coupled with mass spectrometry, we show that the C-terminal intrinsically disordered tail of TCPTP functions as an intramolecular autoinhibitor"],"journal":["Nature communications"],"pubmed_title":["The catalytic activity of TCPTP is auto-regulated by its intrinsically disordered tail and activated by Integrin alpha-1."],"pmcid":["PMC8748766"],"funding_grant_id":["R01 NS091336","R01 GM098482"],"pubmed_authors":["Hsu SD","Li Y","Peti W","Meng TC","Chen YY","Page R","Singh JP"],"additional_accession":[]},"is_claimable":false,"name":"The catalytic activity of TCPTP is auto-regulated by its intrinsically disordered tail and activated by Integrin alpha-1.","description":"T-Cell Protein Tyrosine Phosphatase (TCPTP, PTPN2) is a non-receptor type protein tyrosine phosphatase that is ubiquitously expressed in human cells. TCPTP is a critical component of a variety of key signaling pathways that are directly associated with the formation of cancer and inflammation. Thus, understanding the molecular mechanism of TCPTP activation and regulation is essential for the development of TCPTP therapeutics. Under basal conditions, TCPTP is largely inactive, although how this is achieved is poorly understood. By combining biomolecular nuclear magnetic resonance spectroscopy, small-angle X-ray scattering, and chemical cross-linking coupled with mass spectrometry, we show that the C-terminal intrinsically disordered tail of TCPTP functions as an intramolecular autoinhibitor","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jan","modification":"2026-05-08T08:32:33.581Z","creation":"2025-05-18T12:10:05.852Z"},"accession":"S-EPMC8748766","cross_references":{"pubmed":["35013194"],"doi":["10.1038/s41467-021-27633-6"]}}