- Design of fast proteolysis-based signaling and logic circuits in mammalian cells

Multilayer design of proteolysis-based signaling pathways a, Two-layer protease-cascade function with a catalytically inactive split tobacco etch virus protease (TEVp*) domain fused to the autoinhibitory CC, showing low leakage and high fold activation (additional data in Supplementary Fig. 11). b, Double inverter consisting of a split TEVp regulated by split PPVp; PPVp is regulated by the rapamycin-induced split SbMVp. c, B nimply A logic function combining human immunodeficiency virus-1 (HIV-1p) and PPVp as input signals. The SQVSQNYPIVQNLQ recognition sequence for HIV-1 protease was used. Transfection plasmid mixtures are listed in Supplementary Tables 1 and 4. Values are the means from three (c) and four (a,b) cell cultures ±s.d. and are representative of at least two independent experiments; significance was tested by one-way ANOVA with Tukey’s comparison between the indicated ON and OFF states (confidence interval, 95%, degrees of freedom, 11; F = 72 (c)).

Go to figure page

Reference

Design of fast proteolysis-based signaling and logic circuits in mammalian cells - Scientific Figure on ResearchGate. Available from: https://www.researchgate.net/figure/Multilayer-design-of-proteolysis-based-signaling-pathways-a-Two-layer-protease-cascade_fig4_329540251 [accessed 18 Mar 2025]

Caption

Multilayer design of proteolysis-based signaling pathways
a, Two-layer protease-cascade function with a catalytically inactive split tobacco etch virus protease (TEVp*) domain fused to the autoinhibitory CC, showing low leakage and high fold activation (additional data in Supplementary Fig. 11). b, Double inverter consisting of a split TEVp regulated by split PPVp; PPVp is regulated by the rapamycin-induced split SbMVp. c, B nimply A logic function combining human immunodeficiency virus-1 (HIV-1p) and PPVp as input signals. The SQVSQNYPIVQNLQ recognition sequence for HIV-1 protease was used. Transfection plasmid mixtures are listed in Supplementary Tables 1 and 4. Values are the means from three (c) and four (a,b) cell cultures ±s.d. and are representative of at least two independent experiments; significance was tested by one-way ANOVA with Tukey’s comparison between the indicated ON and OFF states (confidence interval, 95%, degrees of freedom, 11; F = 72 (c)).

Embed code

<a href="https://www.researchgate.net/figure/Multilayer-design-of-proteolysis-based-signaling-pathways-a-Two-layer-protease-cascade_fig4_329540251"><img src="https://www.researchgate.net/publication/329540251/figure/fig4/AS:731591114489907@1551436322631/Multilayer-design-of-proteolysis-based-signaling-pathways-a-Two-layer-protease-cascade.png" alt="Multilayer design of proteolysis-based signaling pathways
a, Two-layer protease-cascade function with a catalytically inactive split tobacco etch virus protease (TEVp*) domain fused to the autoinhibitory CC, showing low leakage and high fold activation (additional data in Supplementary Fig. 11). b, Double inverter consisting of a split TEVp regulated by split PPVp; PPVp is regulated by the rapamycin-induced split SbMVp. c, B nimply A logic function combining human immunodeficiency virus-1 (HIV-1p) and PPVp as input signals. The SQVSQNYPIVQNLQ recognition sequence for HIV-1 protease was used. Transfection plasmid mixtures are listed in Supplementary Tables 1 and 4. Values are the means from three (c) and four (a,b) cell cultures ±s.d. and are representative of at least two independent experiments; significance was tested by one-way ANOVA with Tukey’s comparison between the indicated ON and OFF states (confidence interval, 95%, degrees of freedom, 11; F = 72 (c))."/></a>