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. 2000 Oct 30;151(3):601–612. doi: 10.1083/jcb.151.3.601

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© 2000 The Rockefeller University Press

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graphic file with name JCB0006045.f6a.jpg — Rabenosyn-5 overexpression impairs cathepsin D trafficking. (A) Time course analysis of cathepsin D trafficking. HeLa cells overexpressing Rabenosyn-5, EEA1, or mock transfected were metabolically labeled with [³⁵S]methionine for 30 min, chased with cold methionine for the indicated times, and then cellular cathepsin D was immunoprecipitated and relative quantities of precursor (left) or processed intermediate (right) cathepsin D were analyzed by SDS-PAGE followed by autoradiography. The signal was quantified by densitometric analysis of the autoradiograms. (B) Effect of overexpression of Rabenosyn-5 truncation mutants upon cathepsin D trafficking. Experiments were performed as described in A, except quantification of relative percentages of precursor cathepsin D (black bars) and processed intermediate cathepsin D (white bars) were performed after 4 h of chase time.

graphic file with name JCB0006045.f6b.jpg — Rabenosyn-5 overexpression impairs cathepsin D trafficking. (A) Time course analysis of cathepsin D trafficking. HeLa cells overexpressing Rabenosyn-5, EEA1, or mock transfected were metabolically labeled with [³⁵S]methionine for 30 min, chased with cold methionine for the indicated times, and then cellular cathepsin D was immunoprecipitated and relative quantities of precursor (left) or processed intermediate (right) cathepsin D were analyzed by SDS-PAGE followed by autoradiography. The signal was quantified by densitometric analysis of the autoradiograms. (B) Effect of overexpression of Rabenosyn-5 truncation mutants upon cathepsin D trafficking. Experiments were performed as described in A, except quantification of relative percentages of precursor cathepsin D (black bars) and processed intermediate cathepsin D (white bars) were performed after 4 h of chase time.