Membrane contact sites regulate vacuolar fission via sphingolipid metabolism
Year: 2023
Type: 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 Saccharomyces cerevisiae . 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.
Source: eLife
Institution: Hiroshima University
Language: English
Subfield: Cell Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $2,500
Awards: Transcriptional regulation of vesicular trafficking through lipid metabolism, Molecular mechanism of ceramide transport via organelle membrane contacts., Mechanisms of protein sorting by glycolipid remodeling, Identification and Functional Characterization of Proteins Newly Implicated in Non-Vesicular Ceramide Transport, Mechanism of nonvesicular lipid domain component transport and significance of multi-transport systems
OpenAlex ID: W4385281681