ArticleThe Journal of biological chemistry2012
Once phosphorylated, tyrosines in carboxyl terminus of protein-tyrosine kinase Syk interact with signaling proteins, including TULA-2, a negative regulator of mast cell degranulation.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 39 citations in OpenAlex.
- Exploring UBASH3A: from immune regulation to autoimmune diseases.Journal of translational medicine · 2025Review
- Role of Tula-Family Proteins in Cell Signaling and Activation: Advances and Challenges.International journal of molecular sciences · 2024Article
- Inactivation of the Sts enzymes promotes resistance to lethalInfection and immunity · 2023Article
- TULA Proteins in Men, Mice, Hens, and Lice: Welcome to the Family.International journal of molecular sciences · 2023Review
- The Sts Proteins: Modulators of Host Immunity.International journal of molecular sciences · 2023Review
- STS1 and STS2 Phosphatase Inhibitor Baicalein Enhances the Expansion of Hematopoietic and Progenitor Stem Cells and Alleviates 5-Fluorouracil-Induced Myelosuppression.International journal of molecular sciences · 2023Article
- TULA-Family Regulators of Platelet Activation.International journal of molecular sciences · 2022Review
- RACK1 plays a critical role in mast cell secretion and Ca2+ mobilization by modulating F-actin dynamics.Journal of cell science · 2021Article
- Siglec-8 Signals Through a Non-Canonical Pathway to Cause Human Eosinophil DeathFrontiers in immunology · 2021Article
- A role for the Sts phosphatases in negatively regulating IFNγ-mediated production of nitric oxide in monocytes.Immunity, inflammation and disease · 2020Article
- An unexpected 2-histidine phosphoesterase activity of suppressor of T-cell receptor signaling protein 1 contributes to the suppression of cell signaling.The Journal of biological chemistry · 2020Article
- Article
- Interplay between HGAL and Grb2 proteins regulates B-cell receptor signaling.Blood advances · 2019Article
- TULA-2 Deficiency Enhances Platelet Functional Responses to CLEC-2 Agonists.TH open : companion journal to thrombosis and haemostasis · 2018Article
- Article
- Unperturbed Immune Function despite Mutation of C-Terminal Tyrosines in Syk Previously Implicated in Signaling and Activity Regulation.Molecular and cellular biology · 2017Article
- Increased Resistance to Intradermal Francisella tularensis LVS Infection by Inactivation of the Sts Phosphatases.Infection and immunity · 2017Article
- Modulating Host Signaling Pathways to Promote Resistance to Infection byFrontiers in cellular and infection microbiology · 2017Review
- Proteome analysis of mast cell releasates reveals a role for chymase in the regulation of coagulation factor XIIIA levels via proteolytic degradation.The Journal of allergy and clinical immunology · 2017Article
- TULA-2 Protein Phosphatase Suppresses Activation of Syk through the GPVI Platelet Receptor for Collagen by Dephosphorylating Tyr(P)346, a Regulatory Site of Syk.The Journal of biological chemistry · 2016Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Activation of the high affinity IgE-binding receptor (FcεRI) results in the tyrosine phosphorylation of two conserved tyrosines located close to the COOH terminus of the protein-tyrosine kinase Syk. Synthetic peptides representing the last 10 amino acids of the tail of Syk with these two tyrosines either nonphosphorylated or phosphorylated were used to precipitate proteins from mast cell lysates. Proteins specifically precipitated by the phosphorylated peptide were identified by mass spectrometry. These included the adaptor proteins SLP-76, Nck-1, Grb2, and Grb2-related adaptor downstream of Shc (GADS) and the protein phosphatases SHIP-1 and TULA-2 (also known as UBASH3B or STS-1). The presence of these in the precipitates was further confirmed by immunoblotting. Using the peptides as probes in far Western blots showed direct binding of the phosphorylated peptide to Nck-1 and SHIP-1. Immunoprecipitations suggested that there were complexes of these proteins associated with Syk especially after receptor activation; in these complexes are Nck, SHIP-1, SLP-76, Grb2, and TULA-2 (UBASH3B or STS-1). The decreased expression of TULA-2 by treatment of mast cells with siRNA increased the FcεRI-induced tyrosine phosphorylation of the activation loop tyrosines of Syk and the phosphorylation of phospholipase C-γ2. There was parallel enhancement of the receptor-induced degranulation and activation of nuclear factor for T cells or nuclear factor κB, indicating that TULA-2, like SHIP-1, functions as a negative regulator of FcεRI signaling in mast cells. Therefore, once phosphorylated, the terminal tyrosines of Syk bind complexes of proteins that are positive and negative regulators of signaling in mast cells.
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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.