Conference – Pierre Lavigne , Wednesday, February 28 at 11:00 a.m.

PROTEO is pleased to invite you on Wednesday, February 28 at 11:00 a.m. to the presentation by Dr. Pierre Lavigne (Université de Sherbrooke), invited by Dr. Christian Salesse and Dr. Élodie Boisselier at Local G1-09, Hôpital du Saint-Sacrement, Centre de recherche du CHU de Québec – Université Laval.

Mechanism of lipid binding and release by START domains: The missing link

The START domains are specialized in the intracellular, non-vesicular and inter-membrane transport of lipids and cholesterol. STARD1 and STARD4 are involved in cholesterol transport to the mitochondria and endoplasmic reticulum, respectively. We have shown that the START domains (STARD5 and STARD6) can also bind and transport bile acids and soluble steroid hormones. The mechanism of binding and release of these ligands has long been poorly understood, as it requires a large conformational change. Indeed, their binding site is deeply embedded within the START domain. Using structural studies by solution NMR and molecular dynamics (simulation and 15N spin relaxation) on several time scales, we have been able to determine the exact nature of this conformational change in STARD6. But what about the inter-membrane transport of cholesterol by STARD1 and STARD4?  The conservation of the primary structure suggests that the conformational change is conserved in all START domains, but solution studies with STARD1 and STARD4 were found to be difficult because of their intrinsic adsorption properties. The aim of this presentation is to establish a collaboration with the groups of Christian Salesse and Élodie Boisselier to study the interactions of STARD4 and STARD1 with lipid monolayers (with or without cholesterol) to better understand the phenomenon of inter-membrane binding and release. This is the missing link!

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