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. 2012 Apr 6;287(22):17975–17984. doi: 10.1074/jbc.M111.310458

FIGURE 4.

FIGURE 4.

α6β4 integrin regulates the translation of α3 integrin through 4EBP1. A, polysome fractions from control keratinocytes or α6 shRNA clone 1 keratinocytes were isolated, and the levels of α3 integrin (left), β4 integrin (middle), and GAPDH (right) mRNA were determined by quantitative RT-PCR, as indicated. The graphs represent the relative levels of α3, β4, or GAPDH mRNA normalized to the ribosomal protein S26 and compared with HEK. The samples were measured in triplicate, and the graphs represent the means ± S.E. of three independent experiments. B, whole cell extracts from wild-type (HEK), α6 shRNA clone 1 cells, or α6 shRNA cone 1 cells induced to re-express α6 integrin (+refα6) were probed for levels of phosphorylated 4EBP1 and total 4EBP1. C and D, whole cell extracts from wild-type (HEK), α6 shRNA clone 1 cells, or α6 shRNA clone 1 cells infected with adenovirus encoding myristoylated AKT were probed for levels of phosphorylated 4EBP1 and total 4EBP1 (C) or β4 integrin and α3 integrin (D). Actin and lamin A/C were used as loading controls in B–D. Graphs in B–D represent the means expression (normalized to lamin A/C) + S.E. of three independent experiments, quantified from immunoblots.