Structural and Functional Asymmetry of Plasma Membranes

Faraday Discussions documents a long-established series of Faraday Discussion meetings which provide a unique international forum for the exchange of views and newly acquired results in developing areas of physical chemistry, biophysical chemistry and chemical physics. The papers presented are published in the Faraday Discussion volume together with a record of the discussion contributions made at the meeting. Faraday Discussions therefore provide an important record of current international knowledge and views in the field concerned. The latest (2022) impact factor of Faraday Discussions is 3.4.

• Plasma membrane asymmetry and lipid homeostasisThe omics era has provided much data on phospholipids, sphingolipids, sterols and proteins located in different membranes, although information on their functional relevance remains limited. This section address challenges such as measuring trans-leaflet lipid distribution, including the spatiotemporal relation to overall lipid composition, and dissecting secondary lipid messengers from lipid ‘players’ with respect to bulk membrane properties.Engineering plasma membrane mimicsQuantification of physicochemical properties of realistic plasma membrane mimics hinges on the controlled production of asymmetric bilayers in the presence and absence of integral or peripheral membrane proteins. This section discusses recently developed asymmetric membrane procedures and how these might be improved.Structure and dynamics of asymmetric membranesThis session seeks to obtain physicochemical insights from lipid-only plasma membrane mimics. The section includes minimum realistic mimics of mammalian or bacterial plasma membranes, as well as the role of cholesterol in tuning and maintaining membrane asymmetry.Proteins in asymmetric membranesThis section focuses on integral proteins functionally reconstituted into asymmetric membranes. Topics will include folding and reconstitution of proteins in asymmetric lipid membranes, control of protein directionality, and stability of lipid asymmetry in the presence of integral proteins.