Oral Session 5
Wednesday, March 31, 2021 | 10:00 - 11:00 EDT | Go to About Oral Sessions to learn more about the session format.
Session Chair: Isabella Felli (CERM University of Florence)
Invited Speakers & Abstracts
Interplay between VAMP2 and lipids in regulation of
SNARE complex assembly studied by in-cell NMR
The synaptic vesicle associated membrane protein 2 (VAMP2), one of the main components of the SNARE complex, regulates the fusion of synaptic vesicles with the presynaptic membrane. Whether and how VAMP2 is associated with membrane in vivo are key questions to understand the regulatory mechanism of VAMP2-mediated SNARE complex assembly. We systemically characterized the membrane binding of VAMP2 in different mammalian cells at residue-resolution using in-cell NMR. Combining with immunofluorescence microscopy, membrane fractionation and solution NMR, we reveal that VAMP2 recognizes different lipid molecules by distinct binding pattern, which results in different influences on VAMP2-mediated SNARE complex assembly. The distinct local lipid environment on the SV membrane fine-tunes the conformation of VAMP2 for SNARE complex assembly and regulates SV trafficking.
Dynamic Protein Complexes in Biology
In biology, signal fidelity is dependent on controlled interactions between a myriad of molecules, very often involving proteins. Here, in their complexes, proteins can retain different degrees of dynamics and maintain flexibility. Contributing to this view, intrinsically disordered proteins (IDPs) with their increased flexibility may form different complexes with different partners and may retain their fast dynamic within complexes, both with other IDPs and with folded domains. With an outset in the complex between Prothymosin alpha and linker histone H1 and including examples with folded domains such as calmodulin, illustrations of how one particular complex may assume a set of different conformations resulting in a broad energy landscapes of the complex and with relevance to its biology, are presented