AI Article Synopsis
- * Deleting tricalbins (Tcb1, Tcb2, and Tcb3) in yeast disrupts the dynamics of vacuole fusion and fission, leading to fragmented vacuoles and an accumulation of the sphingolipid precursor phytosphingosine (PHS).
- * Restoring the connection between the nucleus and vacuole improves vacuolar structure by allowing PHS to be transported properly, highlighting the importance of MCSs in maintaining vacuole shape through sphingolipid metabolism.
Article Abstract
Membrane contact sites (MCSs) are junctures that perform important roles including coordinating lipid metabolism. Previous studies have indicated that vacuolar fission/fusion processes are coupled with modifications in the membrane lipid composition. However, it has been still unclear whether MCS-mediated lipid metabolism controls the vacuolar morphology. Here, we report that deletion of tricalbins (Tcb1, Tcb2, and Tcb3), tethering proteins at endoplasmic reticulum (ER)-plasma membrane (PM) and ER-Golgi contact sites, alters fusion/fission dynamics and causes vacuolar fragmentation in the yeast . In addition, we show that the sphingolipid precursor phytosphingosine (PHS) accumulates in tricalbin-deleted cells, triggering the vacuolar division. Detachment of the nucleus-vacuole junction (NVJ), an important contact site between the vacuole and the perinuclear ER, restored vacuolar morphology in both cells subjected to high exogenous PHS and Tcb3-deleted cells, supporting that PHS transport across the NVJ induces vacuole division. Thus, our results suggest that vacuolar morphology is maintained by MCSs through the metabolism of sphingolipids.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10972560 | PMC |
| http://dx.doi.org/10.7554/eLife.89938 | DOI Listing |
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