Copper blocks V‐ATPase activity and SNARE complex formation to inhibit yeast vacuole fusion
| العنوان: | Copper blocks V‐ATPase activity and SNARE complex formation to inhibit yeast vacuole fusion |
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| المؤلفون: | Katherine D. Sullivan, David A. Rivera-Kohr, Gregory E. Miner, Rutilio A. Fratti, Brandon C. Jones, Chi Zhang, Logan R. Hurst, Matthew L. Starr, Annie Guo |
| المصدر: | Traffic |
| بيانات النشر: | Wiley, 2019. |
| سنة النشر: | 2019 |
| مصطلحات موضوعية: | Cytoplasm, Saccharomyces cerevisiae Proteins, Vesicular Transport Proteins, chemistry.chemical_element, Vacuole fusion, Saccharomyces cerevisiae, Vacuole, Biology, Membrane Fusion, Biochemistry, Article, 03 medical and health sciences, 0302 clinical medicine, Structural Biology, Genetics, V-ATPase, Chelation, Molecular Biology, 030304 developmental biology, Adenosine Triphosphatases, 0303 health sciences, Cell Membrane, Lipid bilayer fusion, Cell Biology, Copper, Cell biology, Membrane, chemistry, Vacuoles, Carrier Proteins, SNARE Proteins, SNARE complex, 030217 neurology & neurosurgery, Molecular Chaperones |
| الوصف: | The accumulation of copper in organisms can lead to altered functions of various pathways and become cytotoxic through the generation of reactive oxygen species. In yeast, cytotoxic metals such as Hg+ , Cd2+ and Cu2+ are transported into the lumen of the vacuole through various pumps. Copper ions are initially transported into the cell by the copper transporter Ctr1 at the plasma membrane and sequestered by chaperones and other factors to prevent cellular damage by free cations. Excess copper ions can subsequently be transported into the vacuole lumen by an unknown mechanism. Transport across membranes requires the reduction of Cu2+ to Cu+ . Labile copper ions can interact with membranes to alter fluidity, lateral phase separation and fusion. Here we found that CuCl2 potently inhibited vacuole fusion by blocking SNARE pairing. This was accompanied by the inhibition of V-ATPase H+ pumping. Deletion of the vacuolar reductase Fre6 had no effect on the inhibition of fusion by copper. This suggests that Cu2+ is responsible for the inhibition of vacuole fusion and V-ATPase function. This notion is supported by the differential effects of chelators. The Cu2+ -specific chelator triethylenetetramine rescued fusion, whereas the Cu+ -specific chelator bathocuproine disulfonate had no effect on the inhibited fusion. |
| تدمد: | 1600-0854 1398-9219 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b524ab6f0a4fe1796704575e2109b095Test https://doi.org/10.1111/tra.12683Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....b524ab6f0a4fe1796704575e2109b095 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 16000854 13989219 |
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