| Literature DB >> 33446409 |
Luis-Carlos Tábara1, Jordan L Morris1, Julien Prudent2.
Abstract
Mitochondria are dynamic organelles that undergo cycles of fission and fusion events depending on cellular requirements. During mitochondrial division, the GTPase dynamin-related protein-1 is recruited to endoplasmic reticulum (ER)-induced mitochondrial constriction sites where it drives fission. However, the events required to complete scission of mitochondrial membranes are not well understood. Here, we emphasize the recently described roles for Golgi-derived phosphatidylinositol 4-phosphate (PI4P)-containing vesicles in the last steps of mitochondrial division. We then propose how trans-Golgi network vesicles at mitochondria-ER contact sites and PI4P generation could mechanistically execute mitochondrial division, by recruiting PI4P effectors and/or the actin nucleation machinery. Finally, we speculate on mechanisms to explain why such a complex dance of different organelles is required to facilitate the remodelling of mitochondrial membranes.Entities:
Keywords: Drp1; PI4P; TGN vesicles; membrane contact sites; mitochondrial division
Mesh:
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Year: 2021 PMID: 33446409 DOI: 10.1016/j.tcb.2020.12.005
Source DB: PubMed Journal: Trends Cell Biol ISSN: 0962-8924 Impact factor: 20.808