Abstract
Down‐regulation of ribosomal protein (RP) genes was observed in myosin II null strains (myo1Δ) of the yeast Saccharomyces cerevisiae, which is likely to be a result of repression of the TOR pathway. We have shown the PKC1 Cell Wall Integrity Pathway (CWIP) is activated in this mutant, the Slt2p/Mpk1p is phosphorylated and it's expression is essential for survival. The objective of this study was to determine whether there is cross‐talk between the PKC1 and TOR signaling pathways in the CWIP response in a myo1Δ strain. To test this, we deleted the ROM1, TOR1 and SIT4 genes in a myo1Δ strain and analyzed the levels of phosphorylated Slt2p/Mpk1p by western blot in single and double mutant strains. Viability assays and growth curves were performed to test for genetic interactions. Preliminary results show that upon rapamycin treatment, rom1Δmyo1Δ, sit4Δmyo1Δ and tor1Δmyo1Δ strains presented decreased levels of phosphorylated Slt2p relative to the treated myo1Δ single mutant. Also, there was a synthetic growth defect in rom1Δmyo1Δ and tor1Δmyo1Δ but not in sit4Δmyo1Δ strains. We concluded that ROM1, TOR1 and SIT4 gene products modulate cross‐talk between the PKC1 and the TOR signaling pathways, and that Rom1p and Tor1p are important to maintain optimal activation of the PKC1 CWIP under cell wall stress conditions. Supported by NIGMS‐NIAID (5SC1AI081658‐02), NCRR‐RCMI (G12RR03051) and MBRS‐RISE (R25GM061838).
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
