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Membrane lipids are lipids involved in forming the structure of biological membranes – both the cell membrane and intracellular membranes – and in membrane function, namely compartmentalization of biological processes. Membrane lipids consist primarily of phospholipids, glycolipids and cholesterol, which can be arranged in bilayers and organized with integral and peripheral membrane proteins to generate functioning membranes.
Droplet interface bilayers can be used as a model of artificial membranes for synthetic biology and drug delivery applications, however, their accessibility using non-invasive techniques remains challenging. Here, the authors develop an in-situ bilayer manipulation of encapsulated droplet interface bilayers in hydrogel capsules, generated by high-order emulsification in monolithic 3D-printed microfluidic devices.
Membrane fusion is crucial for fabricating artificial membranes. Here, the authors present an approach combining electric field with hydraulic pressure to physically control the fusion, enabling tuning of the shape and size of the 3D freestanding lipid bilayers in physiological solutions.
Phosphorylation of ACSL4 by mitochondria-located metabolic kinase PCK2 is critical to regulating ferroptosis-associated phospholipid remodeling in tumor-repopulating cells that are resistant to chemotherapy and radiotherapy.
The study describes the molecular structure of the human histamine 2 receptor in active conformation and in complex with Gs heterotrimer, synthesized in a cell-free system and co-translationally inserted into preformed nanodiscs.
Adipose triglyceride lipase (ATGL), an enzyme in fatty acid metabolism, was identified as a negative regulator of the noncanonical inflammasome. ATGL binds to lipopolysaccharide and catalyzes the hydrolysis of fatty acid side chains blocking inflammasome activation.
Annexins are calcium-regulated membrane binding proteins with an array of cellular activities. Here, Gerke et al. describe recent research highlighting the many functions of annexins and provide a view on directions for the future.
Ferroptosis, a cell death mechanism induced by lipid peroxidation, is pivotal in tumor suppression. A recent study shows that tumor repopulating cells evade ferroptosis and develop resistance to therapy via subverting a lipid metabolism enzyme.
The coenzyme Q biosynthetic pathway has evaded full characterization for decades, in part due to the inherent insolubility of coenzyme Q and the instability of its membrane-associated biosynthetic enzymes. Now, researchers have resurrected an active ancestral coenzyme Q metabolon in vitro that has unveiled valuable insights into previously uncharacterized aspects of coenzyme Q biosynthesis.
Screening of a chemical library identifies a novel ferroptosis inhibitor that directly interferes with the formation of intracellular membrane contacts between the endoplasmic reticulum (ER) and mitochondria (ERMCS), commonly referred to as mitochondria-associated membranes (MAMs).
New cryo-electron microscopy (cryo-EM) structures of CDP- and CDP-choline-bound choline phosphotransferase 1 (CHPT1) and choline/ethanolamine phosphotransferase 1 (CEPT1), involved in the metabolism of the two main lipids in eukaryotic cell membranes, capture the membrane proteins at resolution <4 Å, sufficient to gain mechanistic insights into these enzymes.