Role of molecular players in endocytosis revealed by neutron scattering: the Clathrin Adaptor CALM
Clathrin-mediated endocytosis (CME) is the main mechanism by which eukaryotic cells internalize and recycle most membrane proteins (termed cargo). It is driven by different Adaptor Proteins which directly link the clathrin scaffold to cargos, and modulated by accessory proteins. Simplifying the system down to its core elements is enabling us to address a number of important questions. The focus on this proposal is on the clathrin-adaptor CALM. The protein possesses an amphipathic Alpha helix that inserts into membranes curvature-induced defects, driving the formation of clathrin-coated pits as well as influencing clathrin-coated vesicle size. However, the modality of the binding and the spatial arrangement of CALM upon lipid interaction is still unclear. A combined Neutron Reflectometry (NR) and Small Angle Neutron Scattering (SANS) approach studying each steps of this process, including the effect of the accessory SNARE protein, will provide a complete physical and thermodynamic description of the collective mechanisms involved. The proposed experiments will form part of the PhD of Andreas Santamaria.
The data is currently only available to download if you are a member of the proposal team.
The recommended format for citing this dataset in a research publication is in the following format:
ZACCAI Nathan; Armando Maestro; MATSARSKAIA Olga; OWEN David J. and SANTAMARIA Andreas. (2021). Role of molecular players in endocytosis revealed by neutron scattering: the Clathrin Adaptor CALM. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-02-918
This data is not yet public
This data is not yet public
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