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Table 2 Relative Phosphorylation Level of Src Substrates in FAK+/+[Src] vs. FAK-/-[Src] Cells

From: Paxillin-Y118 phosphorylation contributes to the control of Src-induced anchorage-independent growth by FAK and adhesion

  Adherent Suspension
v-Src Substrates Similar levela More in FAK+/+
More in FAK-/-
Similar level More in FAK+/+
More in FAK-/-
Vinculin (poY100)   5 – 6    7 – 8  
p190RhoGAP (poY)*    1.5 – 2    1.5 – 2
Shc (poY239/poY240) Yes    Yes   
Sam68 (poY)*    2 Yes   
PLC-γ1 (poY783) Yes    Yes   
PKC-δ (poY311)    2 Yes   
Paxillin (poY118)    4    10
Paxillin (poY31) Yes     2 – 3  
Eps8 (poY)*, b Yes    Yes   
p56 Dok-2 (poY351)   5     2
Crk (poY)*    2    2
Cortactin (poY421)c Yes     2  
Connexin43 (poY265)d    2   2–3  
p120Catenin (poY228)   2     2
p130 CAS (poY410)   2    2  
Annexin II (poY)* Yes    Yes   [3]e
  1. *blotting with mAb 4G10 anti-PTyr was used to ascertain the level of tyrosine phosphorylation after immunoprecipitation with substrate-specific Abs.
  2. astatistically equal level of relative substrate phosphorylation between FAK+/+[Src] and FAK-/-[Src] cells, based on triplicate experiments. Relative phosphorylation for a given experiment is calculated as the phospho- substrate signal normalized to total substrate protein level, then normalized to loading control proteins. Note that Src transformation increases GAPDH protein levels ~2-fold and decreases actin protein level ~2-fold in the FAK+/+ background in adherent cells only.
  3. bfor both 97 kDa and 68 kDa Eps8 isoforms.
  4. cin adherent cultures, the 80 kDa cortactin isoform protein level is reduced in the absence of FAK, but the relative phosphorylation levels are similar.
  5. dconnexin-43 (poY265) levels were not normalized.
  6. erelative decrease in phospho-annexin II levels in suspended FAK-/-[v-Src] cells.