AI Article Synopsis
- Kes1/Osh4, part of the oxysterol binding protein-related superfamily, is crucial for controlling cell-cycle activities, specifically inhibiting the G/S transition in nutrient-poor conditions and promoting aging.* -
- This regulation relies on the kinase Rim15 and counteracts the actions of Sec14, indicating a complex interaction independent of their membrane-trafficking roles.* -
- The study suggests that Kes1 acts as a target for the NuA4 acetyltransferase, linking lipid signaling with cell-cycle control and proposing that ORPs may function like tumor suppressors in this process.*
Article Abstract
Kes1/Osh4 is a member of the conserved, but functionally enigmatic, oxysterol binding protein-related protein (ORP) superfamily that inhibits phosphatidylinositol transfer protein (Sec14)-dependent membrane trafficking through the trans-Golgi (TGN)/endosomal network. We now report that Kes1, and select other ORPs, execute cell-cycle control activities as functionally non-redundant inhibitors of the G/S transition when cells confront nutrient-poor environments and promote replicative aging. Kes1-dependent cell-cycle regulation requires the Greatwall/MASTL kinase ortholog Rim15, and is opposed by Sec14 activity in a mechanism independent of Kes1/Sec14 bulk membrane-trafficking functions. Moreover, the data identify Kes1 as a non-histone target for NuA4 through which this lysine acetyltransferase co-modulates membrane-trafficking and cell-cycle activities. We propose the Sec14/Kes1 lipid-exchange protein pair constitutes part of the mechanism for integrating TGN/endosomal lipid signaling with cell-cycle progression and hypothesize that ORPs define a family of stage-specific cell-cycle control factors that execute tumor-suppressor-like functions.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6444186 | PMC |
| http://dx.doi.org/10.1016/j.devcel.2017.12.026 | DOI Listing |
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