Tumor Progression Locus 2 Mediates Signal-Induced Increases in Cytoplasmic Calcium and Cell Migration

Maria Hatziapostolou, Georgios Koukos, Christos Polytarchou, Filippos Kottakis, Oksana Serebrennikova, Athan Kuliopulos, Philip N. Tsichlis*

*To whom correspondence should be addressed. E-mail: ptsichlis{at}tuftsmedicalcenter.org

This PDF file includes:

• Table S1. Statistical differences between samples 25 s after treatment with thrombin.
• Table S2. Statistical differences between samples 25 s after treatment with PAR1 agonist.
• Fig. S1. Gα_i2 promotes phosphorylation of ERK1/2 through Tpl2.
• Fig. S2. Phosphorylation and activation of classical and novel PKCs by thrombin depends on Tpl2.
• Fig. S3. The phosphorylation of classical PKCs after thrombin stimulation depends on Gα_i2.
• Fig. S4. PKC inhibition attenuates thrombin-induced ERK1/2 phosphorylation but not Ca²⁺ signals.
• Fig. S5. Expression profile of PLCβ isoforms in Rec-WT and Rec-EV cells.
• Fig. S6. Thrombin-induced PLCβ₃ phosphorylation at Ser⁵³⁷ depends on Tpl2.
• Fig. S7. Specificity of the antibody that recognizes PLCβ₃ phosphorylated at Ser⁵³⁷.
• Fig. S8. The knockdown of Gβ₁, Gβ₂, or Gβ₃, singly or in combination, interferes only partially with thrombin-induced ERK phosphorylation and Ca²⁺ signals.
• Fig. S9. Number of cells before and after thrombin stimulation.
• Fig. S10. ERK and JNK phosphorylation by S1P in immortalized MEFs and BMDMs is Tpl2-dependent.
• Fig. S11. The increase in cytoplasmic Ca²⁺, induced by Wnt5a and IL-1β, but not TNF-α, depends on Tpl2.
  

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