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Akbulut, Simge; Reddi, Alagarsamy L.; Aggarwal, Priya; Ambardekar, Charuta; Canciani, Barbara; Kim, Marianne K.H.; Hix, Laura; Vilimas, Tomas; Mason, Jacqueline; Basson, M. Albert; Lovatt, Matthew; Powell, Jonathan; Collins, Samuel; Quatela, Steven; Phillips, Mark; Licht, Jonathan D.

Sprouty Proteins Inhibit Receptor-mediated Activation of Phosphatidylinositol-specific Phospholipase C

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  • Medientyp: E-Artikel
  • Titel: Sprouty Proteins Inhibit Receptor-mediated Activation of Phosphatidylinositol-specific Phospholipase C
  • Beteiligte: Akbulut, Simge; Reddi, Alagarsamy L.; Aggarwal, Priya; Ambardekar, Charuta; Canciani, Barbara; Kim, Marianne K.H.; Hix, Laura; Vilimas, Tomas; Mason, Jacqueline; Basson, M. Albert; Lovatt, Matthew; Powell, Jonathan; Collins, Samuel; Quatela, Steven; Phillips, Mark; Licht, Jonathan D.
  • Erschienen: American Society for Cell Biology (ASCB), 2010
  • Erschienen in: Molecular Biology of the Cell
  • Sprache: Englisch
  • DOI: 10.1091/mbc.e10-02-0123
  • ISSN: 1059-1524; 1939-4586
  • Schlagwörter: Cell Biology ; Molecular Biology
  • Entstehung:
  • Anmerkungen:
  • Beschreibung: <jats:p>Sprouty (Spry) proteins are negative regulators of receptor tyrosine kinase signaling; however, their exact mechanism of action remains incompletely understood. We identified phosphatidylinositol-specific phospholipase C (PLC)-γ as a partner of the Spry1 and Spry2 proteins. Spry–PLCγ interaction was dependent on the Src homology 2 domain of PLCγ and a conserved N-terminal tyrosine residue in Spry1 and Spry2. Overexpression of Spry1 and Spry2 was associated with decreased PLCγ phosphorylation and decreased PLCγ activity as measured by production of inositol (1,4,5)-triphosphate (IP<jats:sub>3</jats:sub>) and diacylglycerol, whereas cells deficient for Spry1 or Spry1, -2, and -4 showed increased production of IP<jats:sub>3</jats:sub>at baseline and further increased in response to growth factor signals. Overexpression of Spry 1 or Spry2 or small-interfering RNA-mediated knockdown of PLCγ1 or PLCγ2 abrogated the activity of a calcium-dependent reporter gene, suggesting that Spry inhibited calcium-mediated signaling downstream of PLCγ. Furthermore, Spry overexpression in T-cells, which are highly dependent on PLCγ activity and calcium signaling, blocked T-cell receptor-mediated calcium release. Accordingly, cultured T-cells from Spry1 gene knockout mice showed increased proliferation in response to T-cell receptor stimulation. These data highlight an important action of Spry, which may allow these proteins to influence signaling through multiple receptors.</jats:p>
  • Zugangsstatus: Freier Zugang