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dc.contributor.authorHuang, J.
dc.contributor.authorMousley, Carl
dc.contributor.authorDacquay, L.
dc.contributor.authorMaitra, N.
dc.contributor.authorDrin, G.
dc.contributor.authorHe, C.
dc.contributor.authorRidgway, N.
dc.contributor.authorTripathi, A.
dc.contributor.authorKennedy, M.
dc.contributor.authorKennedy, B.
dc.contributor.authorLiu, W.
dc.contributor.authorBaetz, K.
dc.contributor.authorPolymenis, M.
dc.contributor.authorBankaitis, V.
dc.identifier.citationHuang, J. and Mousley, C. and Dacquay, L. and Maitra, N. and Drin, G. and He, C. and Ridgway, N. et al. 2018. A Lipid Transfer Protein Signaling Axis Exerts Dual Control of Cell-Cycle and Membrane Trafficking Systems. Developmental Cell.

© 2017 Elsevier Inc. 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 1 /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. Huang et al. demonstrate the yeast oxysterol-binding protein (ORP) homolog Kes1, and other ORPs, are inhibitors of the G 1 /S transition. They show that Kes1 is a non-histone target for the NuA4 lysine acetyltransferase and participates in a phosphatidylinositol-4-phopshate-dependent mechanism for integrating TGN/endosomal lipid signaling with cell-cycle progression.

dc.publisherCell Press
dc.titleA Lipid Transfer Protein Signaling Axis Exerts Dual Control of Cell-Cycle and Membrane Trafficking Systems
dc.typeJournal Article
dcterms.source.titleDevelopmental Cell
curtin.departmentSchool of Pharmacy and Biomedical Sciences
curtin.accessStatusFulltext not available

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