Plasma Membrane Protein Nce102 Modulates Morphology and Function of the Yeast Vacuole
| Autor: | Jan Malinsky, Maria Balazova, Katarina Vaskovicova, Petra Veselá, Dagmar Folkova, Jakub Zahumensky |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Cell vacuolar morphology lcsh:QR1-502 Saccharomyces cerevisiae Vacuole yeast Biochemistry Article lcsh:Microbiology 03 medical and health sciences 0302 clinical medicine medicine Molecular Biology Eisosome 030304 developmental biology 0303 health sciences Chemistry Lipid microdomain membrane microdomains eisosome sphingolipid metabolism Sphingolipid Yeast Cell biology medicine.anatomical_structure Membrane Membrane protein Vacuoles 030217 neurology & neurosurgery |
| Zdroj: | Biomolecules, Vol 10, Iss 1476, p 1476 (2020) Biomolecules; Volume 10; Issue 11; Pages: 1476 Biomolecules |
| Popis: | Membrane proteins are targeted not only to specific membranes in the cell architecture, but also to distinct lateral microdomains within individual membranes to properly execute their biological functions. Yeast tetraspan protein Nce102 has been shown to migrate between such microdomains within the plasma membrane in response to an acute drop in sphingolipid levels. Combining microscopy and biochemistry methods, we show that upon gradual ageing of a yeast culture, when sphingolipid demand increases, Nce102 migrates from the plasma membrane to the vacuole. Instead of being targeted for degradation it localizes to V-ATPase-poor, i.e., ergosterol-enriched, domains of the vacuolar membrane, analogous to its plasma membrane localization. We discovered that, together with its homologue Fhn1, Nce102 modulates vacuolar morphology, dynamics, and physiology. Specifically, the fusing of vacuoles, accompanying a switch of fermenting yeast culture to respiration, is retarded in the strain missing both proteins. Furthermore, the absence of either causes an enlargement of ergosterol-rich vacuolar membrane domains, while the vacuoles themselves become smaller. Our results clearly show decreased stability of the V-ATPase in the absence of either Nce102 or Fhn1, a possible result of the disruption of normal microdomain morphology of the vacuolar membrane. Therefore, the functionality of the vacuole as a whole might be compromised in these cells. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|