Elimination of plasma membrane phosphatidylinositol (4,5)-bisphosphate is required for exocytosis from mast cells

Hammond, Gerald; Dove, Stephen K.; Nicol, Alastair; Pinxteren, Jef; Zicha, Daniel; Schiavo, Giampietro

doi:10.1242/jcs.02912

Cited by 62 publications

(61 citation statements)

References 74 publications

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“…These results indicate that PIP5K-Iγ negatively regulates a step in FcεRI signaling that contributes to stimulated exocytosis in a PKC-independent manner. These results are consistent with previous observations indicating a negative downstream role for PtdIns(4,5)P 2 in degranulation by rat peritoneal mast cells (Hammond et al, 2006). Further studies will be necessary to characterize the nature and mechanism of this negative regulatory pathway.…”

Section: Ptdins(45)p 2 Generated By Pip5k-iγ Functions As Plc Substratesupporting

confidence: 92%

The β- and γ-isoforms of type I PIP5K regulate distinct stages of Ca2+ signaling in mast cells

Vasudevan

Jeromin

Volpicelli‐Daley

et al. 2009

Journal of Cell Science

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Crosslinking of IgE receptors by antigen initiates Ca2+ mobilization in mast cells by activating phospholipase-Cγ-mediated hydrolysis of phosphatidylinositol-4,5-bisphosphate [PtdIns(4,5)P2]. The resulting inositol 1,4,5-trisphosphate-mediated Ca2+ release from the endoplasmic reticulum (ER) activates store-operated Ca2+ entry, which is necessary for exocytotic release of inflammatory mediators. To investigate roles for PtdIns(4,5)P2-synthesizing isozymes of the type I phosphatidylinositol 4-phosphate 5-kinase family (PIP5K-I) in mast cell signaling, we compared the ectopic expression of wild-type and catalytically inactive PIP5K-Iβ in RBL-2H3 mast cells. Surprisingly, both antigen and thapsigargin-stimulated Ca2+ influx were reduced by overexpression of active PIP5K-Iβ, whereas antigen-stimulated Ca2+ release from ER stores was unaffected. Consistent with these results, Ca2+ entry stimulated by antigen or thapsigargin was enhanced by expression of a plasma-membrane-associated inositol polyphosphate 5′-phosphatase, whereas antigen-stimulated Ca2+ release from stores was reduced. To investigate the role of PIP5K-Iγ in antigen-stimulated Ca2+ mobilization, we used bone-marrow-derived mast cells from PIP5K-Iγ–/– mice. Antigen-stimulated Ca2+ release from ER stores was substantially reduced in the absence of PIP5K-Iγ, but thapsigargin-mediated Ca2+ entry was unaffected. In summary, PIP5K-Iγ positively regulates antigen-stimulated Ca2+ release from ER stores, whereas PIP5K-Iβ negatively regulates store-operated Ca2+ entry, suggesting that these different PIP5K-I isoforms synthesize functionally distinct pools of PtdIns(4,5)P2 at the plasma membrane.

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Section: Ptdins(45)p 2 Generated By Pip5k-iγ Functions As Plc Substratesupporting

confidence: 92%

The β- and γ-isoforms of type I PIP5K regulate distinct stages of Ca2+ signaling in mast cells

Vasudevan

Jeromin

Volpicelli‐Daley

et al. 2009

Journal of Cell Science

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“…Nuclei were stained with 5 µM Hoechst 33342 dye in 0.05 M Tris-HCl pH 7.4 for 2 min in the dark at room temperature. The specificity of PI(4,5)P2 staining was verified by the use of neomycin as reported by Hammond et al (2006).…”

Section: Immunofluorescencementioning

confidence: 75%

SHIP2 controls plasma membrane PI(4,5)P2 thereby participating in the control of cell migration in 1321 N1 glioblastoma cells

Edimo

Ghosh

Derua

et al. 2016

Journal of Cell Science

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Phosphoinositides, particularly phosphatidylinositol (3,4,5)-trisphosphate [PI(3,4,5)P3] and phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2], are recognized by SHIP2 (also known as INPPL1) a member of the inositol polyphosphate 5-phosphatase family. SHIP2 dephosphorylates PI(3,4,5)P3 to form PI(3,4)P2; the latter interacts with specific target proteins (e.g. lamellipodin). Although the preferred SHIP2 substrate is PI(3,4,5)P3, PI(4,5)P2 can also be dephosphorylated by this enzyme to phosphatidylinositol 4-phosphate (PI4P). Through depletion of SHIP2 in the glioblastoma cell line 1321 N1, we show that SHIP2 inhibits cell migration. In different glioblastoma cell lines and primary cultures, SHIP2 staining at the plasma membrane partly overlaps with PI(4,5)P2 immunoreactivity. PI(4,5)P2 was upregulated in SHIP2-deficient N1 cells as compared to control cells; in contrast, PI4P was very much decreased in SHIP2-deficient cells. Therefore, SHIP2 controls both PI(3,4,5)P3 and PI(4,5)P2 levels in intact cells. In 1321 N1 cells, the PI(4,5)P2-binding protein myosin-1c was identified as a new interactor of SHIP2. Regulation of PI(4,5)P2 and PI4P content by SHIP2 controls 1321 N1 cell migration through the organization of focal adhesions. Thus, our results reveal a new role of SHIP2 in the control of PI(4,5)P2, PI4P and cell migration in PTEN-deficient glioblastoma 1321 N1 cells.

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“…By doing so, PtdIns(3,4,5) P 3 , PtdIns(4,5)P 2 , and PtdIns(4)P at the plasma membrane were visualized in fi xed cells. However, this method allows only one species of PI to be stained ( 19,34,39 ), and it is important to analyze a number of PIs simultaneously because cellular events are coordinately controlled by different PI species. Our method allows visualization of three different PIs in stimulated cells, and the spatial resolution is much improved compared with the method using GFPfusion PH domains.…”

Section: Discussionmentioning

confidence: 99%

Quantification and visualization of phosphoinositides by quantum dot-labeled specific binding-domain probes

Irino

Tokuda

Hasegawa

et al. 2012

Journal of Lipid Research

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This article is available online at http://www.jlr.org enzymes is associated with disorders such as diabetes and cancer, which suggests that cellular concentrations of each PI species is usually under strict control ( 4,5 ).A number of PI-binding domains have been identifi ed, including pleckstrin homology (PH); Phox (PX); Fab1, YOTB, Vac1p, and EEA1 (FYVE); Epsin N-terminal homology (ENTH); and Glucosyltransferase, Rab-like GTPase activator, and myotubularin (GRAM) domains ( 6, 7 ). Although most PH domains show little specifi city in the PIs they bind, several show relatively high specifi city; these include the PH domains of phospholipase C ␦ 1 (PLC ␦ 1) for PtdIns(4,5)P 2 and the general receptor for phosphoinositides-1 (GRP1) for PtdIns(3,4,5)P 3 ( 8, 9 ). In addition, the tandem-PH domain-containing protein-1 (TAPP1) and the four phosphate-adaptor protein-1 (FAPP1) PH domains specifi cally bind PtdIns(3,4)P 2 and PtdIns4P, respectively ( 10, 11 ). Other domains that bind specifi c PIs have also been described. The FYVE domains of hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs) and early endosome antigen-1 (EEA1) specifi cally recognize PtdIns3P, which is primarily found in endosomes, multivesicular bodies, and phagosomes ( 12 ). The GRAM domains of myotubularin and myotubularin-related protein 2 (MTMR2) are involved in endosomal and vacuolar targeting through interaction with PtdIns(3,5)P 2 ( 13 ). Moreover, some PI-binding domains have functions beyond simply recruiting host proteins to the membrane surface. Such domains, including ENTH, Bin Amphiphysin Rvs (BAR), and FCH and BAR (F-BAR), bind PIs with little specifi city and participate in endocytosis, cytokinesis, and Press, February 3, 2012 DOI 10.1194 Quantifi cation and visualization of phosphoinositides by quantum dot-labeled specifi c binding-domain probes Abbreviations: CHO-IR , Chinese hamster ovary cells expressing the wild-type human insulin receptor; CHO-IR, GFP, green fl uorescent protein; GRP1, general receptor for phosphoinositides-1; PC, phosphatidylcholine; PDGF, platelet-derived growth factor; PE, phosphatidylethanolamine; PH, pleckstrin homology; PI, phosphoinositide; PI3K, PI 3-kinase; PLC ␦ 1, phospholipase C ␦ 1; Qdot, quantum dot; ROI, region of interest; TAPP-1, tandem-PH domain-containing protein-1. Published, JLR Papers in

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Elimination of plasma membrane phosphatidylinositol (4,5)-bisphosphate is required for exocytosis from mast cells

Cited by 62 publications

References 74 publications

The β- and γ-isoforms of type I PIP5K regulate distinct stages of Ca2+ signaling in mast cells

The β- and γ-isoforms of type I PIP5K regulate distinct stages of Ca2+ signaling in mast cells

SHIP2 controls plasma membrane PI(4,5)P2 thereby participating in the control of cell migration in 1321 N1 glioblastoma cells

Quantification and visualization of phosphoinositides by quantum dot-labeled specific binding-domain probes

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