Resultados de investigación

15 pages, 3 figures, 6 tables, Supporting information for the article https://doi.org/10.1021/acsomega.3c00816, Materials and methods.-- Figures.-- Tables.-- References, Peer reviewed

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Stephanie J. Wilson ... et al.-- 1 file, These data were compiled from original and published datasets of coastal groundwater / subterranean estuary research efforts along global coastline (sites within 1km of shoreline). The dataset includes sampling site names, locations, original sample information, sample depth, temperature, salinity, dissolved nitrogen concentrations, and dissolved phosphorus concentrations. The data source or curator is also included in the dataset, Australian Research Council (ARC), grant/award no. DE140101733, DP120101645, FT170100327; Knut and Alice Wallenberg Foundation, grant/award no. 2022.0096; National Science Foundation (NSF), grant/award no. 1658135, 1737258; Swedish Research Council (VR), grant/award no. 2020-00457, Peer reviewed

1 file, This dataset comprises input data from INTECMAR and the predicted outcomes, The authors gratefully acknowledge the financial support by the Programa de axudas á etapa predoutoral da Xunta de Galicia (Axencia Galega de Innovación) (Grant nº IN606A-2022/025). F.F.P. and A.V. were supported by REDEIRA (TED2021-132188B-I00) project, funded by MCIN/AEI/10.13039/501100011033, Peer reviewed

Same conditions as in S1 Table. We found Cbk1 described interactions in cdc15-2 cells in the absence (A “cdc15-2 vs. control”), the presence of rapamycin (B “cdc15-2 + rapa vs. ctrl”), and TOR1-1 cdc15-2 cells after the addition of rapamycin (C “TOR1-1 cdc15-2 + rapa vs. ctrl”). In all cases, cells were arrested in late anaphase after having been grown at 37 °C. Three biological replicates of each described cells and conditions were performed and compared with 3 biological replicates of untagged control cells (ctrlCounts). Cbk1 interactions can be found in: https://thebiogrid.org/35668/summary/saccharomyces-cerevisiae/cbk1.html., Peer reviewed

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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., Peer reviewed

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., Peer reviewed

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., Peer reviewed

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