ArticleProceedings of the National Academy of Sciences of the United States of America1993
Stimulation by phospholipids of a protein-tyrosine-phosphatase containing two src homology 2 domains.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 106 citations in OpenAlex.
- A Multimodal Imaging Pipeline for the Discovery of Molecular Markers of Cellular Neighborhoods.bioRxiv : the preprint server for biology · 2026Article
- SHP-1 tyrosine phosphatase binding to c-Src kinase phosphor-dependent conformations: A comparative structural framework.PloS one · 2023Article
- Alterations in cellular and organellar phospholipid compositions of HepG2 cells during cell growth.Scientific reports · 2021Article
- Dysregulated Lipid Metabolism and Its Role in α-Synucleinopathy in Parkinson's Disease.Frontiers in neuroscience · 2019Review
- CD22: A Regulator of Innate and Adaptive B Cell Responses and Autoimmunity.Frontiers in immunology · 2018Review
- Crystal structure of human protein tyrosine phosphatase SHP-1 in the open conformation.Journal of cellular biochemistry · 2011Article
- Characterization of cellular DGK-theta.Advances in enzyme regulation · 2010Article
- Characterization of a highly effective protein substrate for analysis of JAK2(V617F) Activity.Experimental hematology · 2007Article
- Src-mediated activation of alpha-diacylglycerol kinase is required for hepatocyte growth factor-induced cell motility.The EMBO journal · 2000Article
- Activation of phosphotyrosine phosphatase activity attenuates mitogen-activated protein kinase signaling and inhibits c-FOS and nitric oxide synthase expression in macrophages infected with Leishmania donovani.Infection and immunity · 1999Article
- Tyrosine phosphatase SHP-2 dephosphorylates the platelet-derived growth factor receptor but enhances its downstream signalling.The Biochemical journal · 1999Article
- The src homology 2-containing inositol phosphatase (SHIP) is the gatekeeper of mast cell degranulation.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Microvesicle release is associated with extensive protein tyrosine dephosphorylation in platelets stimulated by A23187 or a mixture of thrombin and collagen.The Biochemical journal · 1998Article
- The phosphotyrosine phosphatase SHP-2 participates in a multimeric signaling complex and regulates T cell receptor (TCR) coupling to the Ras/mitogen-activated protein kinase (MAPK) pathway in Jurkat T cells.The Journal of experimental medicine · 1998Article
- Relocalization of phospholipase D activity mediates membrane formation during meiosis.The Journal of cell biology · 1998Article
- Interleukin 1-beta-induced protein kinase C-zeta activation is mimicked by exogenous phospholipase D.The Biochemical journal · 1997Article
- Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST.Molecular and cellular biology · 1996Article
- CD22 associates with protein tyrosine phosphatase 1C, Syk, and phospholipase C-gamma(1) upon B cell activation.The Journal of experimental medicine · 1996Article
- Phosphatidic acid activation of protein kinase C-zeta overexpressed in COS cells: comparison with other protein kinase C isotypes and other acidic lipids.The Biochemical journal · 1994Article
- Phorbol ester-induced expression, phosphorylation, and translocation of protein-tyrosine-phosphatase 1C in HL-60 cells.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
PTP1C, a protein-tyrosine-phosphatase (protein-tyrosine-phosphate phosphohydrolase, EC 3.1.3.48) containing two src homology 2 domains, is poorly active when assayed with various protein substrates in vitro. Its activity is stimulated > 1000-fold by anionic phospholipids when myelin basic protein or mitogen-activated protein kinase is used as substrate but reduced in the presence of several other substrates. Data are presented to indicate a direct interaction of the enzyme with phospholipids. Enzyme stimulation directed only toward certain specific substrates is interpreted by assuming that these compounds also bind to the phospholipid vesicles where they will be subjected to rapid enzymatic attack. A possible regulation of PTP1C by its translocation to the cell membrane is hypothesized.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.