ArticleMolecular and cellular biology2004
Activation of RBL-2H3 mast cells is dependent on tyrosine phosphorylation of phospholipase D2 by Fyn and Fgr.
Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Allergenic protein-induced type I hypersensitivity models: a review.Frontiers in allergy · 2024Review
- Phospholipase D2 in prostate cancer: protein expression changes with Gleason score.British journal of cancer · 2019Article
- Phospholipase D and Its Essential Role in Cancer.Molecules and cells · 2017Review
- Amygdala-Hippocampal Phospholipase D (PLD) Signaling As Novel Mechanism of Cocaine-Environment Maladaptive Conditioned Responses.The international journal of neuropsychopharmacology · 2016Article
- Phospholipase D in cell signaling: from a myriad of cell functions to cancer growth and metastasis.The Journal of biological chemistry · 2014Review
- Phosphatidic acid, phospholipase D and tumorigenesis.Advances in biological regulation · 2014Article
- The exquisite regulation of PLD2 by a wealth of interacting proteins: S6K, Grb2, Sos, WASp and Rac2 (and a surprise discovery: PLD2 is a GEF).Cellular signalling · 2011Review
- The Src family kinase Fgr is critical for activation of mast cells and IgE-mediated anaphylaxis in mice.Journal of immunology (Baltimore, Md. : 1950) · 2011Article
- Mast cell biology: introduction and overview.Advances in experimental medicine and biology · 2011Review
- An emerging role for the lipid mediator sphingosine-1-phosphate in mast cell effector function and allergic disease.Advances in experimental medicine and biology · 2011Review
- Regulation of mast cell responses in health and disease.Critical reviews in immunology · 2011Review
- Loss of TRPC1-mediated Ca2+ influx contributes to impaired degranulation in Fyn-deficient mouse bone marrow-derived mast cells.Journal of leukocyte biology · 2010Article
- The molecular basis of phospholipase D2-induced chemotaxis: elucidation of differential pathways in macrophages and fibroblasts.Molecular and cellular biology · 2010Article
- New concepts in phospholipase D signaling in inflammation and cancer.TheScientificWorldJournal · 2010Review
- A comprehensive model that explains the regulation of phospholipase D2 activity by phosphorylation-dephosphorylation.Molecular and cellular biology · 2010Article
- The tyrosine kinase network regulating mast cell activation.Immunological reviews · 2009Review
- Article
- The elucidation of novel SH2 binding sites on PLD2.Oncogene · 2006Article
- The uncovering of a novel regulatory mechanism for PLD2: formation of a ternary complex with protein tyrosine phosphatase PTP1B and growth factor receptor-bound protein GRB2.Biochemical and biophysical research communications · 2005Article
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Authors and funding
9 authors.
Funding
Abstract
Both phospholipase D1 (PLD1) and PLD2 regulate degranulation when RBL-2H3 cells are stimulated via the immunoglobulin E receptor, Fc epsilon RI. However, the activation mechanism for PLD2 is unclear. As reported here, PLD2 but not PLD1 is phosphorylated through the Src kinases, Fyn and Fgr, and this phosphorylation appears to regulate PLD2 activation and degranulation. For example, only hemagglutinin-tagged PLD2 was tyrosine phosphorylated in antigen-stimulated cells that had been made to express HA-PLD1 and HA-PLD2. This phosphorylation was blocked by a Src kinase inhibitor or by small interfering RNAs directed against Fyn and Fgr and was enhanced by overexpression of Fyn and Fgr but not by other Src kinases. The phosphorylation and activity of PLD2 were further enhanced by the tyrosine phosphatase inhibitor, Na(3)VO(4). Mutation of PLD2 at tyrosines 11, 14, 165, or 470 partially impaired, and mutation of all tyrosines blocked, PLD2 phosphorylation and activation, although two of these mutations were detrimental to PLD2 function. PLD2 phosphorylation preceded degranulation, both events were equally sensitive to inhibition of Src kinase activity, and both were enhanced by coexpression of PLD2 and the Src kinases. The findings provide the first description of a mechanism for activation of PLD2 in a physiological setting and of a role for Fgr in Fc epsilon RI-mediated signaling.
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