Abstract
The Target Of Rapamycin (TOR) signaling pathway is known to regulate growth in response to nutrient availability and stress in eukaryotic cells. In the present study, we have investigated the TOR pathway in the white-rot fungus Phanerochaete chrysosporium. Inhibition of TOR activity by rapamycin affects conidia germination and hyphal growth highlighting the conserved mechanism of susceptibility to rapamycin. Interestingly, the secreted protein content is also affected by the rapamycin treatment. Finally, homologs of the components of TOR pathway can be identified in P. chrysosporium. Altogether, those results indicate that the TOR pathway of P. chrysosporium plays a central role in this fungus.
Highlights
The Target Of Rapamycin (TOR) signaling pathway is highly conserved among eukaryotes and regulates essential cellular processes including protein synthesis, ribosome biogenesis, autophagy, and cytoskeleton organization [1]
Rapamycin binds to FK506 Binding Protein 12 (FKBP12) and the FK506 Rapamycin Binding (FRB) domain of TOR resulting in the inhibition of the TOR kinase activity and cell growth arrest
We found that the TOR pathway play a central role in P. chrysosporium
Summary
The Target Of Rapamycin (TOR) signaling pathway is highly conserved among eukaryotes and regulates essential cellular processes including protein synthesis, ribosome biogenesis, autophagy, and cytoskeleton organization [1]. The serine/threonine-protein kinase TOR, firstly identified in Saccharomyces cerevisiae [7] is the central component of the TOR signaling pathway. This kinase interacts with other partners to form two multiprotein complexes named TORC1 and TORC2. Both complexes regulate their targets by phosphorylation. Of these two complexes, only TORC1 is sensitive to rapamycin [8,9].
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
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.
