A Lipid Transfer Protein Signaling Axis Exerts Dual Control of Cell-Cycle and Membrane Trafficking Systems
| Autor: | Wenshe R. Liu, Michael A. Kennedy, Neale D. Ridgway, Vytas A. Bankaitis, Nairita Maitra, Ashutosh Tripathi, Kristin Baetz, Carl J. Mousley, Guillaume Drin, Jin Huang, Chong He, Louis Dacquay, Michael Polymenis, Brian K. Kennedy |
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| Přispěvatelé: | Institut de pharmacologie moléculaire et cellulaire (IPMC), Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Centre National de la Recherche Scientifique (CNRS), Buck Institute |
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Receptors Steroid Saccharomyces cerevisiae Proteins Endosome [SDV]Life Sciences [q-bio] Golgi Apparatus Endosomes Saccharomyces cerevisiae Biology General Biochemistry Genetics and Molecular Biology Article Cell membrane 03 medical and health sciences 0302 clinical medicine Cell Movement medicine [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Phospholipid Transfer Proteins Molecular Biology Phosphatidylinositol transfer protein ComputingMilieux_MISCELLANEOUS Histone Acetyltransferases Kinase Cell Cycle Cell Membrane Membrane Proteins Biological Transport Cell Biology Lipid signaling Lipids Cell biology 030104 developmental biology medicine.anatomical_structure Membrane protein Oxysterol binding Signal transduction 030217 neurology & neurosurgery Developmental Biology Signal Transduction |
| Zdroj: | Developmental Cell Developmental Cell, Elsevier, 2018, 44 (3), pp.378-391.e5. ⟨10.1016/j.devcel.2017.12.026⟩ |
| ISSN: | 1534-5807 |
| DOI: | 10.1016/j.devcel.2017.12.026⟩ |
| Popis: | 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 Great-wall/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. |
| Databáze: | OpenAIRE |
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