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. 2012 May;14(5):396–409. doi: 10.1596/neo.111514

Figure 5.

Figure 5

Figure 5

(A) Representative Western blots showing the level of ubiquitinated proteins in EGFcyt and mock cells. In the presence of EGFcyt and mbEGFctF, the level of ubiquitinated total protein and protein fractions derived from subcellular compartments was increased. This enhanced protein ubiquitination was not observed with EGFdel23 (not shown) and mock. Ponceau S-stained blots served as loading control. EGFR served as marker for the membrane fraction, β-actin for the total and cytoplasmic fraction and histone 1 (H1) as marker for the nuclear fraction. (B) Transfection with a specific siUCH-L1 (50 nM) construct for 72 and 96 hours successfully silenced UCH-L1 expression in UCH-L1+ mock cells. (C) Western blot analysis showed that silencing of UCH-L1 protein coincided with increased levels of total ubiquitinated (Ub-) proteins in siUCH-L1 treated mock compared with UCH-L1+ mock and UCH-L1- EGFcyt cells treated with scrambled siRNA.