Auxiliary proteins play functional roles in modulating the assembly and activity of a non-canonical ABC transporter that is important for the maintenance of outer membrane lipid asymmetry.

Identification of how bioactive lipids bind and inhibit glycine transporters has the potential to be exploited in the development of a new class of analgesics for chronic pain.

An outer membrane vesicle pulse-chase assay demonstrates that the Acinetobacter baumannii Mla system is a retrograde lipid transporter.

Structures of a TMEM16 phospholipid scramblase reveal that its Ca²⁺-dependent activation entails global conformational changes and how these rearrangements affect the membrane to enable transbilayer lipid transfer.

Structure of MlaFEDB ABC transporter with substrate bound in the outward-open pocket of MlaE provides mechanistic insights into lipid transport within the Gram-negative bacterial cell envelope.

Differences in the lipid solvation energetics of associated and dissociated states is a primary driving force for membrane protein oligomerization, presenting a molecular mechanism for lipid regulation in biology.

GRAMD1 proteins sense a transient expansion of the accessible pool of plasma membrane cholesterol and facilitate its transport to the endoplasmic reticulum at ER-PM contact sites.

Yeast specific lipids promote the transport of lipid transfer protein (LTP) across the blood brain barrier to the neurons that regulate systemic insulin signaling.

Native mass spectrometry reveals the thermodynamic basis for high-affinity lipid binding to the ABC transporter MsbA.

An Acinetobacter baumannii ABC transporter likely facilitates transport of glycerophospholipids from the inner to the outer membrane.