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Journal Article
Tyrosine 766 in the fibroblast growth factor receptor-1 is required for FGF-stimulation of phospholipase C, phospholipase D, phospholipase A(2), phosphoinositide 3-kinase and cytoskeletal reorganisation in porcine aortic endothelial cells
M.J. Cross, M.N. Hodgkin, S. Roberts, E. Landgren, M.J. Wakelam, L. Claesson-Welsh
Journal of Cell Science 2000 113: 643-651;
M.J. Cross
Department of Genetics, Rudbeck Laboratory, S-75185 Uppsala, Sweden.
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M.N. Hodgkin
Department of Genetics, Rudbeck Laboratory, S-75185 Uppsala, Sweden.
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S. Roberts
Department of Genetics, Rudbeck Laboratory, S-75185 Uppsala, Sweden.
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E. Landgren
Department of Genetics, Rudbeck Laboratory, S-75185 Uppsala, Sweden.
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M.J. Wakelam
Department of Genetics, Rudbeck Laboratory, S-75185 Uppsala, Sweden.
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L. Claesson-Welsh
Department of Genetics, Rudbeck Laboratory, S-75185 Uppsala, Sweden.
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Summary

Fibroblast growth factor-mediated signalling was studied in porcine aortic endothelial cells expressing either wild-type fibroblast growth factor receptor-1 or a mutant receptor (Y766F) unable to bind phospholipase C-(γ). Stimulation of cells expressing the wild-type receptor resulted in activation of phospholipases C, D and A(2) and increased phosphoinositide 3-kinase activity. Stimulation of the wild-type receptor also resulted in stress fibre formation and a cellular shape change. Cells expressing the Y766F mutant receptor failed to stimulate phospholipase C, D and A(2) as well as phosphoinositide 3-kinase. Furthermore, no stress fibre formation or shape change was observed. Both the wild-type and Y766F receptor mutant activated MAP kinase and elicited proliferative responses in the porcine aortic endothelial cells. Thus, fibroblast growth factor receptor-1 mediated activation of phospholipases C, D and A(2) and phosphoinositide 3-kinase was dependent on tyrosine 766. Furthermore, whilst tyrosine 766 was not required for a proliferative response, it was required for fibroblast growth factor receptor-1 mediated cytoskeletal reorganisation.

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REFERENCES

    1. Ahmed, A.,
    2. Plevin, R.,
    3. Shoaibi, M. A.,
    4. Fountain, S. A.,
    5. Ferriani, R. A. and
    6. Smith, S. K.
    (1994). Basic FGF activates phospholipase D in endothelial cells in the absence of inisitol-lipid hydrolysis. Am. J. Physiol 266, 206–.
    OpenUrl
    1. Chellaiah, M.,
    2. Fitzgerald, C.,
    3. Alvarez, U. and
    4. Hruska, K.
    (1998). C-Src is required for stimulation of gelsolin-associated phosphatidylinositol 3-kinase. J. Biol. Chem 19, 11908–11916.
    OpenUrl
    1. Claesson-Welsh, L.,
    2. Eriksson, A.,
    3. Moren, A.,
    4. Severinsson, L.,
    5. Ek, B.,
    6. Östman, A.,
    7. Betsholtz, C. and
    8. Heldin, C.-H.
    (1988). cDNA cloning and expression of a human platelet-derived growth factor (PDGF) receptor specific for B-chain-containing PDGF molecules. Mol. Cell. Biol 8, 3476–3486.
    OpenUrlAbstract/FREE Full Text
    1. Clyman, R. I.,
    2. Peters, K. G.,
    3. Chen, Y. Q.,
    4. Escobedo, J.,
    5. Williams, L. T.,
    6. Ives, H. E. and
    7. Wilson, E.
    (1994). Phospholipase C-activation, phosphotidylinositol hydrolysis, and calcium mobilization are not required for FGF receptor-mediated chemotaxis. Cell. Adhes. Commun 1, 333–342.
    OpenUrlCrossRefPubMedWeb of Science
    1. Cook, S. J.,
    2. Briscoe, C. P. and
    3. Wakelam, M. J. O.
    (1991). The regulation of phospholipase D activity and its role in sn-1,2-diradylglycerol formation in bombesin-and phorbol 12-myristate 13-acetate-stimulated Swiss 3T3 cells. Biochem. J 280, 431–438.
    OpenUrlAbstract/FREE Full Text
    1. Cross, M. J.,
    2. Roberts, S.,
    3. Ridley, A. J.,
    4. Hodgkin, M. N.,
    5. Stewart, A.,
    6. Claesson-Welsh, L. and
    7. Wakelam, M. J. O.
    (1996). Stimulation of actin stress fibre formation mediated by activation of phospholipase D. Curr. Biol 6, 588–597.
    OpenUrlCrossRefPubMedWeb of Science
    1. Divecha, N. and
    2. Irvine, R. F.
    (1995). Phospholipid signalling. Cell 80, 269–278.
    OpenUrlCrossRefPubMedWeb of Science
    1. Hall, H.,
    2. Williams, E. J.,
    3. Moore, S. E.,
    4. Walsh, F. S.,
    5. Prochiantz, A. and
    6. Doherty, P.
    (1996). Inhibition of FGF-stimulated phosphatidylinositol hydrolysis and neurite outgrowth by a cell-membrane permeable phosphopeptide. Curr. Biol 6, 580–587.
    OpenUrlCrossRefPubMedWeb of Science
    1. Hartwig, J. H.,
    2. Bokoch, G. M.,
    3. Carpenter, C. L.,
    4. Janmey, P. A.,
    5. Taylor, L. A.,
    6. Toker, A. and
    7. Stossel, T. P.
    (1995). Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell 82, 643–653.
    OpenUrlCrossRefPubMedWeb of Science
    1. Hawkins, P. T.,
    2. Eguinoa, A.,
    3. Qiu, R. G.,
    4. Stokoe, D.,
    5. Cooke, F. T.,
    6. Walters, R.,
    7. Wennström, S.,
    8. Claesson-Welsh, L.,
    9. Evans, T.,
    10. Symons, M. and
    11. Stephens, L. R.
    (1995). PDGF stimulates an increase in GTP-Rac via activation of phosphoinositide 3-kinase. Curr. Biol 5, 393–403.
    OpenUrlCrossRefPubMedWeb of Science
    1. Hess, J. A.,
    2. Ji, Q.-S.,
    3. Carpenter, G. and
    4. Exton, J. H.
    (1998). Analysis of platelet-derived growth factor-induced phospholipase D activation in mouse embryo fibroblasts lacking phospholipase C-1. J. Biol. Chem 273, 20517–20524.
    OpenUrlAbstract/FREE Full Text
    1. Huang, J.,
    2. Mohammadi, M.,
    3. Rodrigues, G. A. and
    4. Schlessinger, J.
    (1995). Reduced activation of RAF-1 and MAP kinase by a fibroblast growth factor receptor mutant deficient in stimulation of phosphatidylinositol hydrolysis. J. Biol. Chem 270, 5065–5072.
    OpenUrlAbstract/FREE Full Text
    1. Jackson, T. R.,
    2. Stephens, L. R. and
    3. Hawkins, P. T.
    (1992). Receptor specificity of growth-factor stimulated synthesis of 3-phosphorylated inositol lipids in Swiss 3T3 cells. J. Biol. Chem 267, 16627–16636.
    OpenUrlAbstract/FREE Full Text
    1. Janmey, P. A.
    (1994). Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly. Annu. Rev. Physiol 56, 169–191.
    OpenUrlCrossRefPubMedWeb of Science
    1. Kodaki, T.,
    2. Woscholski, R.,
    3. Hallberg, B.,
    4. Rodriguez-Viciana, P.,
    5. Downward, J. and
    6. Parker, P. J.
    (1994). The activation of phosphatidylinositol 3-kinase by Ras. Curr. Biol 4, 798–806.
    OpenUrlCrossRefPubMedWeb of Science
    1. Kouhara, H.,
    2. Hadari, Y. R.,
    3. Spivak-Kroizman, T.,
    4. Schilling, J.,
    5. Bar-Sagi, D.,
    6. Lax, I. and
    7. Schlessinger, J.
    (1997). A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway. Cell 89, 693–702.
    OpenUrlCrossRefPubMedWeb of Science
    1. Kramer, R. M.,
    2. Roberts, E. F.,
    3. Manetta, J. and
    4. Putnam, J. E.
    (1991). The Ca2+sensitive cytosolic phospholipase A2is a 100-kDa protein in human monoblast U937 cells. J. Biol. Chem 266, 5268–5272.
    OpenUrlAbstract/FREE Full Text
    1. Landgren, E.,
    2. Blume-Jensen, P.,
    3. Courtneidge, S. A. and
    4. Claesson-Welsh, L.
    (1995). Fibroblast growth factor receptor-1 regulation of Src family kinases. Oncogene 10, 2027–2035.
    OpenUrlPubMed
    1. Landgren, E.,
    2. Klint, P.,
    3. Yokote, K. and
    4. Claesson-Welsh, L.
    (1998). Fibroblast growth factor receptor-1 mediates chemotaxis independently of direct SH2-domain protein binding. Oncogene 17, 283–291.
    OpenUrlCrossRefPubMedWeb of Science
    1. Larsson, H.,
    2. Klint, P.,
    3. Landgren, E. and
    4. Claesson-Welsh, L.
    (1999). Fibroblast growth factor receptor-1-mediated endothelial cell proliferation is dependent on the Src homology (SH) SH2/SH3 domain-containing adaptor protein Crk. J. Biol. Chem 274, 25726–25734.
    OpenUrlAbstract/FREE Full Text
    1. Leslie, C. C.,
    2. Voelker, D. R.,
    3. Channon, J. Y.,
    4. Wall, M. M. and
    5. Zelarney, P. T.
    (1988). Properties and purification of an arachidonoyl-hydrolyzing phospholipase A2from a macrophage cell line, RAW 264.7. Biochim. Biophys. Acta 963, 476–492.
    OpenUrlPubMed
    1. Lu, P.-J.,
    2. Shieh, W.-R.,
    3. Rhee, S. G.,
    4. Yin, H. L. and
    5. Chen, C.-H.
    (1996). Lipid products of phosphoinositide 3-kinase bind human profilin with high affinity. Biochemistry 35, 14027–14034.
    OpenUrlCrossRefPubMed
    1. Mohammadi, M.,
    2. Dikic, I.,
    3. Sorokin, A.,
    4. Burgess, W. H.,
    5. Jaye, M. and
    6. Schlessinger, J.
    (1996). Identification of six novel autophosphorylation sites on fibroblast growth factor receptor 1 and elucidation of theirimportance in receptor activation and signal transduction. Mol. Cell. Biol 16, 977–989.
    OpenUrlAbstract/FREE Full Text
    1. Mohammadi, M.,
    2. Dionne, C. A.,
    3. Li, W.,
    4. Li, N.,
    5. Spivak, T.,
    6. Honegger, A. M.,
    7. Jaye, M. and
    8. Schlessinger, J.
    (1992). Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis. Nature 358, 681–684.
    OpenUrlCrossRefPubMedWeb of Science
    1. Mohammadi, M.,
    2. Honegger, A. M.,
    3. Rotin, D.,
    4. Fischer, R.,
    5. Bellot, F.,
    6. Li, W.,
    7. Dionne, C. A.,
    8. Jaye, M.,
    9. Rubinstein, M. and
    10. Schlessinger, J.
    (1991). A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-1. Mol. Cell. Biol 11, 5068–5078.
    OpenUrlAbstract/FREE Full Text
    1. Molloy, C. J.,
    2. Bottaro, D. P.,
    3. Fleming, M. S.,
    4. Gibbs, J. B. and
    5. Aaronson, S.A.
    (1989). PDGF induction of tyrosine phosphorylation of the GTPase activating protein. Nature 342, 711–714.
    OpenUrlCrossRefPubMedWeb of Science
    1. Nemenoff, R. A.,
    2. Winitz, S.,
    3. Qian, N. X.,
    4. Van Putten, V.,
    5. Johnson, G. L. and
    6. Heasley, L. E.
    (1993). Phosphorylation and activation of a high molecular weight form of phospholipase A2by p42 microtubule-associated protein 2 kinase and protein kinase C. J. Biol. Chem 268, 1960–1964.
    OpenUrlAbstract/FREE Full Text
    1. Peppelenbosch, M. P.,
    2. Qiu, R. G.,
    3. de Vries-Smits, A. M.,
    4. Tertoolen, L. G.,
    5. de Laat, S. W.,
    6. McCormick, F.,
    7. Hall, A.,
    8. Symons, M. H. and
    9. Bos, J. L.
    (1995). Rac mediates growth factor-induced arachidonic acid release. Cell 81, 849–856.
    OpenUrlCrossRefPubMedWeb of Science
    1. Peters, K. G.,
    2. Marie, J.,
    3. Wilson, E.,
    4. Ives, H. E.,
    5. Escobedo, J.,
    6. Del Rosario, M.,
    7. Mirda, D. and
    8. Williams, L. T.
    (1992). Point mutation of an FGF receptor abolishes phosphatidylinositol turnover and Ca2+flux but not mitogenesis. Nature 358, 678–681.
    OpenUrlCrossRefPubMed
    1. Plevin, R.,
    2. Palmer, S.,
    3. Gardner, S. and
    4. Wakelam, M. J. O.
    (1990). Regulation of bombesin-stimulated inositol 1,4,5-trisphosphate generation in Swiss 3T3 fibroblasts by a guanine-nucleotide binding protein. Biochem. J 268, 605–610.
    OpenUrlAbstract/FREE Full Text
    1. Ridley, A. J.,
    2. Paterson, H. F.,
    3. Johnston, C. L.,
    4. Diekmann, D. and
    5. Hall, A.
    (1992). The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70, 401–410.
    OpenUrlCrossRefPubMedWeb of Science
    1. Rodriguez-Viciana, P.,
    2. Warne, P. H.,
    3. Dhand, R.,
    4. Vanhaesebroeck, B.,
    5. Gout, I.,
    6. Fry, M. J.,
    7. Waterfield, M. D. and
    8. Downward, J.
    (1994). Phosphatidylinositol-3-OH kinase as a direct target of Ras. Nature 370, 527–532.
    OpenUrlCrossRefPubMedWeb of Science
    1. Sa, G. and
    2. Fox, P. L.
    (1994). Basic fibroblast growth factor-stimulated endothelial cell movement is mediated by a pertussis toxin-sensitive pathway regulating phospholipase A2activity. J. Biol. Chem 269, 3219–3225.
    OpenUrlAbstract/FREE Full Text
    1. Songyang, Z.,
    2. Shoelson, S. E.,
    3. Chaudhuri, M.,
    4. Gish, G.,
    5. Pawson, T.,
    6. Haser, W. G.,
    7. King, F.,
    8. Roberts, T.,
    9. Ratnofsky, S.,
    10. Lechleider, R. J.,
    11. et al.
    (1993). SH2 domains recognize specific phosphopeptide sequences. Cell 72, 767–778.
    OpenUrlCrossRefPubMedWeb of Science
    1. Sorokin, A.,
    2. Mohammadi, M.,
    3. Huang, J. and
    4. Schlessinger, J.
    (1994). Internalization of fibroblast growth factor receptor is inhibited by a point mutation at tyrosine 766. J. Biol. Chem 269, 17056–17061.
    OpenUrlAbstract/FREE Full Text
    1. Spivak-Kroizman, T.,
    2. Mohammadi, M.,
    3. Hu, P.,
    4. Jaye, M.,
    5. Schlessinger, J. and
    6. Lax, I.
    (1994). Point mutation in the fibroblast growth factor receptoreliminates phosphatidylinositol hydrolysis without affecting neuronal differentiation of PC12 cells. J. Biol. Chem 269, 14419–14423.
    OpenUrlAbstract/FREE Full Text
    1. Stephens, L. R.,
    2. Jackson, T. R. and
    3. Hawkins, P. T.
    (1993). Agonist-stimulated synthesis of phosphatidylinositol(3,4,5)-trisphosphate: a new intracellular signalling system?. Biochim. Biophys. Acta 1179, 27–75.
    OpenUrlCrossRefPubMed
    1. Stewart, A.,
    2. Jackson, C. G. and
    3. Wakelam, M. J. O.
    (1997). The regulation by phosphorylation of ‘priming’ of phospholipase A2activity in the neutrophil model system, differentiated HL60 cells. Br. J. Pharmacol 122, 13–20.
    OpenUrlCrossRefPubMed
    1. Toullec, D.,
    2. Pianetti, P.,
    3. Coste, H.,
    4. Bellevergue, P.,
    5. Grand-Perett, T.,
    6. Ajakane, M.,
    7. Baudet, V.,
    8. Boissin, P.,
    9. Boursier, E.,
    10. Loriolle, F.,
    11. Duhamel, L.,
    12. Charon, D. and
    13. Kirilovsky, J.
    (1991). The bisindolymaleimide GF 109203X is a potent and selective inhibitor of Protein Kinase C. J. Biol.Chem 266, 15771–15781.
    OpenUrlAbstract/FREE Full Text
    1. Ullrich, A. and
    2. Schlessinger, J.
    (1990). Signal transduction by receptors with tyrosine kinase activity. Cell 61, 203–212.
    OpenUrlCrossRefPubMedWeb of Science
    1. Vainikka, S.,
    2. Joukov, V.,
    3. Wennström, S.,
    4. Bergman, M.,
    5. Pelicci, P. G. and
    6. Alitalo, K.
    (1994). Signal transduction by fibroblast growth factor receptor-4 (FGFR-4). Comparison with FGFR-1. J. Biol. Chem 269, 18320–18326.
    OpenUrlAbstract/FREE Full Text
    1. van Dijk, M. C. and
    2. van Blitterswijk, W. J.
    (1998). Lipid metabolism in fibroblast growth factor-stimulated L6 myoblasts: a receptor mutation (Y766F) abrogates phospholipase D and diacylglycerol kinase activities. Biochim. Biophys. Acta 1391, 273–279.
    OpenUrlPubMed
    1. van Weering, D. H.,
    2. de Rooij, J.,
    3. Marte, B.,
    4. Downward, J.,
    5. Bos, J. L. and
    6. Burgering, B. M.
    (1998). Protein kinase B activation and lamellipodium formation are independent phosphoinositide 3-kinase-mediated events differentially regulated by endogenous Ras. Mol. Cell. Biol 18, 1802–1811.
    OpenUrlAbstract/FREE Full Text
    1. Virdee, K.,
    2. Brown, B. L. and
    3. Dobson, P. R.
    (1994). Stimulation of arachidonic-acid release from Swiss 3T3 cells by recombinant basic fibroblast growth factor: independence from phosphoinositide turnover. Biochim. Biophys. Acta 1220, 171–180.
    OpenUrlPubMed
    1. Wennström, S.,
    2. Hawkins, P.,
    3. Cooke, F.,
    4. Hara, K.,
    5. Yonezawa, K.,
    6. Kasuga, M.,
    7. Jackson, T.,
    8. Claesson-Welsh, L. and
    9. Stephens, L.
    (1994). Activation of phosphoinositide 3-kinase is required for PDGF-stimulated membrane ruffling. Curr. Biol 4, 385–393.
    OpenUrlCrossRefPubMedWeb of Science
    1. Wennström, S.,
    2. Landgren, E.,
    3. Blume-Jensen, P. and
    4. Claesson-Welsh, L.
    (1992). The platelet-derived growth factor-receptor kinase insert confers specific signaling properties to a chimeric fibroblast growth factor receptor. J. Biol. Chem 267, 13749–13756.
    OpenUrlAbstract/FREE Full Text
    1. Wennström, S.,
    2. Sandström, C. and
    3. Claesson-Welsh, L.
    (1991). cDNA cloning and expression of a human FGF receptor which binds acidic and basic FGF. Growth Factors 4, 197–208.
    OpenUrlCrossRefPubMed
    1. Wong, N. S.,
    2. Barker, C. J.,
    3. Morris, A. J.,
    4. Craxton, A.,
    5. Kirk, C. J. and
    6. Michell, R. H.
    (1992). The inositol phosphates in WRK1 rat mammary tumour cells. Biochem. J 286, 459–468.
    OpenUrlAbstract/FREE Full Text
    1. Xu, H.,
    2. Lee, K. W. and
    3. Goldfarb, M.
    (1998). Novel recognition motif on fibroblast growth factor receptor mediates direct association and activation of SNT adapter proteins. J. Biol. Chem 273, 17987–17990.
    OpenUrlAbstract/FREE Full Text
    1. Yeo, E. J.,
    2. Kazlauskas, A. and
    3. Exton, J. H.
    (1994). Activation of phospholipase C-is necessary for stimulation of phospholipase D by platelet-derived growth factor. J. Biol. Chem 269, 27823–27826.
    OpenUrlAbstract/FREE Full Text
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Tyrosine 766 in the fibroblast growth factor receptor-1 is required for FGF-stimulation of phospholipase C, phospholipase D, phospholipase A(2), phosphoinositide 3-kinase and cytoskeletal reorganisation in porcine aortic endothelial cells
M.J. Cross, M.N. Hodgkin, S. Roberts, E. Landgren, M.J. Wakelam, L. Claesson-Welsh
Journal of Cell Science 2000 113: 643-651;
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Journal Article
Tyrosine 766 in the fibroblast growth factor receptor-1 is required for FGF-stimulation of phospholipase C, phospholipase D, phospholipase A(2), phosphoinositide 3-kinase and cytoskeletal reorganisation in porcine aortic endothelial cells
M.J. Cross, M.N. Hodgkin, S. Roberts, E. Landgren, M.J. Wakelam, L. Claesson-Welsh
Journal of Cell Science 2000 113: 643-651;

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An interview with Derek Walsh

Professor Derek Walsh is the guest editor of our new special issue Cell Biology of Host-Pathogen Interactions. In an interview, Derek tells us about his work in the field of DNA viruses, the impact of the pandemic on virology and what his role as Guest Editor taught him.


How to improve your scientific writing

"If you are a scientist and you want to succeed, you must become a writer."

How do scientists become master storytellers? We called on our journal Editors, proofreaders and contributors to our community sites for their advice on how to improve your scientific writing.


Meet the preLighters: Jennifer Ann Black

Following the theme of our latest special issue, postdoc Jennifer Ann Black studies replication stress and genome plasticity in Leishmania in Professor Luiz Tosi’s lab in Sao Paolo. We caught up with Jenn (virtually) to hear about her relocation to Brazil mid-pandemic, her research on parasites and what she enjoys about ‘preLighting’.

In our special issue, Chandrakar et al. and Rosazza et al. present their latest work on Leishmania.


Mole – The Corona Files

“There are millions of people around the world who continue to believe that the Terrible Pandemic is a hoax.”

Mole continues to offer his wise words to researchers on how to manage during the COVID-19 pandemic.


JCS and COVID-19

For more information on measures Journal of Cell Science is taking to support the community during the COVID-19 pandemic, please see here.

If you have any questions or concerns, please do not hestiate to contact the Editorial Office.

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