Consignes du stage M1S2

 

Bonjour,

Merci de déposer votre/vos proposition(s) de stage pour le master BSIB 2022-2023.

Il n'y a qu'un seul formulaire pour les 3 stages :

  • en M1S2 : à définir pour 2022-2023
  • en M2S3 : à définir pour 2022-2023
  • en M2S4 : à définir pour 2022-2023

Nous souhaitons coupler le stage M2S3 et le stage M2S4, c'est à dire que nous souhaiterions que les 2 stages se déroulent dans la même équipe sur la même thématique. Le stage M2S3 serait donc une période de préparation du stage M2S4. Cette période de stage M2S3 pourrait alors être essentiellement un travail bibliographique et de planification. C'est une recommendation pas une obligation.

pour lire les consignes concernant les 3 stages, merci de suivre les liens ci-après : M1S2, M2S3, M2S4.

Stage Master

  • Stage M2S4

Responsable de l'équipe d'accueil

Loquet
Antoine
This email address is being protected from spambots. You need JavaScript enabled to view it.
0540002212

Personne encadrant le stage (*)

(*) modifiez si une autre personne encadre l'étudiant

Loquet
Antoine
0540002212

Lieu du stage

IECB (Institut Européen de Chimie et Biologie) - Bordeaux

Sujet du stage

Structural study of a synaptic vesicle protein and its interaction with lipid membranes by Nuclear Magnetic Resonance
Context: Synaptotagmin (SYT) is a synaptic vesicle protein that regulates neurotransmission. It is the principal Ca2+ sensor for neuroexocytosis at most nerve terminals. SYT is a single-pass transmembrane protein, abundantly expressed in synaptic vesicles and neurosecretory granules. Voltage–gated calcium influx induces a rapid conformational change in the cytosolic domain of SYT oligomers that bind to anionic phospholipids as well as to the SNARE complex, participating in bilayer deformation culminating in vesicle fusion and neurotransmitter release. Lipids are essential components of the exo-endocytic machinery for neurotransmitter release. They are involved in crucial steps such as vesicle biogenesis, transport, recruitment, membrane organization and deformation, fusion of secretory vesicles with plasma membranes, residence lifetime of specific proteins at the cell surface, endocytosis and recycling. In synapses, lipids such as cholesterol, sphingosine, phosphatidic acid or phosphoinositides of the inner plasma membrane leaflet affect the spatial distribution and/or function of proteins essential for synaptic vesicle exocytosis.

Objectives: We aim at investigating the SYT conformation in a near-native membrane environment, as well as studying specific interaction between SYT and lipids such as gangliosides and cholesterol. We will use solid-state NMR to decipher these interactions and provide an atomic view of SYT-membranes interplay.

Techniques: Structural biology - lipid biophysics - membrane reconstitution

Laboratory: The Master project will take place at the IECB (Institut Européen de Chimie et Biologie) located in Bordeaux, in the team of Antoine Loquet. The team is expert in the development of nuclear magnetic resonance to study biomolecular mechanisms. The project is part of a national collaboration with the teams of O. El Far (Marseille, expert in molecular neruscience) and N. Vitale (Strasbourg, expert in lipid signaling). A continuation of this project into a PhD thesis is planned for 2023.

Contact : Antoine LOQUET
Mail: This email address is being protected from spambots. You need JavaScript enabled to view it.
Website: http://www.loquetlab.org/

Recent publications of the team:
Protein resonance assignment by solid-state NMR based on 1H-detected 13C double-quantum spectroscopy at fast MAS.
Lends et al., J Biomol NMR. 2021
Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective. Daskalov et al., Front Mol Neurosci. 2021
Structural and molecular basis of cross-seeding barriers in amyloids. Daskalov et al., Proc Natl Acad Sci U S A. 2021
Novel self-replicating α-synuclein polymorphs that escape ThT monitoring can spontaneously emerge and acutely spread in neurons.
De Giorgi et al., Sci Adv. 2020
Structural dissection of amyloid aggregates of TDP-43 and its C-terminal fragments TDP-35 and TDP-16. Shenoy et al., FEBS J. 2020
Molecular architecture of bacterial amyloids in Bacillus biofilms. El Mammeri et al., FASEB J. 2019