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- W4386280669 endingPage "e3002263" @default.
- W4386280669 startingPage "e3002263" @default.
- W4386280669 abstract "The target of rapamycin (TOR) signalling pathway plays a key role in the coordination between cellular growth and the cell cycle machinery in eukaryotes. The underlying molecular mechanisms by which TOR might regulate events after anaphase remain unknown. We show for the first time that one of the 2 TOR complexes in budding yeast, TORC1, blocks the separation of cells following cytokinesis by phosphorylation of a member of the NDR (nuclear Dbf2-related) protein-kinase family, the protein Cbk1. We observe that TORC1 alters the phosphorylation pattern of Cbk1 and we identify a residue within Cbk1 activation loop, T574, for which a phosphomimetic substitution makes Cbk1 catalytically inactive and, indeed, reproduces TORC1 control over cell separation. In addition, we identify the exocyst component Sec3 as a key substrate of Cbk1, since Sec3 activates the SNARE complex to promote membrane fusion. TORC1 activity ultimately compromises the interaction between Sec3 and a t-SNARE component. Our data indicate that TORC1 negatively regulates cell separation in budding yeast by participating in Cbk1 phosphorylation, which in turn controls the fusion of secretory vesicles transporting hydrolase at the site of division." @default.
- W4386280669 created "2023-08-31" @default.
- W4386280669 creator A5006884115 @default.
- W4386280669 creator A5021685489 @default.
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- W4386280669 creator A5081946504 @default.
- W4386280669 creator A5088958035 @default.
- W4386280669 date "2023-08-30" @default.
- W4386280669 modified "2023-10-06" @default.
- W4386280669 title "TOR complex 1 negatively regulates NDR kinase Cbk1 to control cell separation in budding yeast" @default.
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