Distinct TORC1 signalling branches regulate Adc17 proteasome assembly chaperone expression

When stressed, cells need to adapt their proteome to maintain protein homeostasis. This requires increased proteasome assembly. Increased proteasome assembly is dependent on increased proteasome assembly chaperone expression. In S. cerevisiae , inhibition of the growth-promoting kinase complex TORC1 causes increased proteasome assembly chaperone expression. This is dependent upon activation of the MAPKinase Mpk1 and relocalisation of assembly chaperone mRNA to patches of dense actin. We show here that TORC1 inhibition alters cell wall properties to induce these changes by activating the Cell Wall Integrity pathway through the Wsc1, Wsc3, and Wsc4 sensor proteins. We demonstrate that in isolation these signals are insufficient to drive protein expression. We identify that the TORC1-activated S6Kinase Sch9 must be inhibited as well. This work expands our knowledge on the signalling pathways which regulate proteasome assembly chaperone expression. Summary TORC1-regulated proteasome assembly chaperone expression is necessary for proteasome assembly and proteostasis. We identify Cell Wall Integrity and Sch9 signalling as mechanisms controlling this.