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Monday 19 March at 11am: Francesca Giordano, Institute for Integrative Biology of the Cell (I2BC), Gif-sur-Yvette. "Staying in touch: ORP-mediated lipid exchange at endoplasmic reticulum-mitochondria membrane contact sites" (Inv. Direction)

Abstract (...)

Abstract Mitochondria are highly dynamic organelles involved in various cellular processes such as energy production, regulation of calcium homeostasis, lipid trafficking and apoptosis. To fulfill all these functions and preserve their morphology and dynamic behavior, mitochondria need to maintain a defined protein and lipid composition in both their membranes. The maintenance of mitochondrial membrane identity requires a selective and regulated transport of specific lipids from/to the endoplasmic reticulum (ER) and across the mitochondria outer and inner membranes. Since they are not integrated in the classical vesicular trafficking routes, mitochondria exchange lipids with the ER at sites of close apposition called membrane contact sites (MCS). Deregulation of such transport activities results in several pathologies including cancer and neurodegenerative disorders. However, the core and regulatory actors of these processes are only beginning to emerge. We have recently shown that the oxysterol-binding protein (OSBP)-related proteins ORP5 and ORP8 – which are known to transport phosphatidylserine (PS) from the ER to the plasma membrane – are novel components of ER-mitochondria MCS and are required for the mantainance of mitochondria morphology and respiratory function [1]. Our recent data show that ORP5/8 constitute the lipid transport machinery at ER-mitochondria MCS and are physically and functionally linked to the components of the MICOS complex that bridge outer and inner mitochondria membrane. By using a combination of imaging methods including electron microscopy together with biochemical and subcellular fractionation approaches, we are studying ORP5/ORP8 function in lipid transport at ER-mitochondria MCS and how they impact on mitochondria morphology, function and dynamics.

1. Galmes, R., et al., ORP5/ORP8 localize to endoplasmic reticulum-mitochondria contacts and are involved in mitochondrial function. EMBO Rep, 2016.
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