Sphingolipids as modulators of membrane proteins.

The diversity of the transmembranome of higher eukaryotes is matched by an enormous diversity of sphingolipid classes and molecular species. The intrinsic properties of sphingolipids are not only suited for orchestrating lateral architectures of biological membranes, but their molecular distinctions also allow for the evolution of protein motifs specifically recognising and interacting with individual lipids. Although various reports suggest a role of sphingolipids in membrane protein function, only a few cases have determined the specificity of these interactions.

Differential transport of Influenza A neuraminidase signal anchor peptides to the plasma membrane.

Influenza A Neuraminidase is essential for virus release from the cell surface of host cells. Given differential structures of the N-terminal sequences including the transmembrane domains of neuraminidase subtypes, we investigated their contribution to transport and localization of subtypes N1, N2 and N8 to the plasma membrane. We generated consensus sequences from all protein entries available for these subtypes.

Mutual recognition of sphingolipid molecular species in membranes.

In membranes liquid disordered (l(d)) and liquid ordered (l(o)) domains can exist that differ in fluidity and function. L(o) areas are predominantly composed of cholesterol and sphingomyelin (SM). Study of the formation of such domains is hampered by a lack of methods to analyze specific lipid-lipid interactions at low concentrations of individual molecular lipid species in membranes.

Specificity of intramembrane protein-lipid interactions.

Our concept of biological membranes has markedly changed, from the fluid mosaic model to the current model that lipids and proteins have the ability to separate into microdomains, differing in their protein and lipid compositions. Since the breakthrough in crystallizing membrane proteins, the most powerful method to define lipid-binding sites on proteins has been X-ray and electron crystallography. More recently, chemical biology approaches have been developed to analyze protein-lipid interactions.