Membrane lipids articles from across Nature Portfolio

The study describes the molecular structure of the human histamine 2 receptor in active conformation and in complex with G_s 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.

A small molecule, CGI1746, was identified to block ferroptosis acting through the sigma-1 receptor, a chaperone primarily at endoplasmic reticulum–mitochondria contacts to mediate calcium transfer.

Mitochondria depend on phospholipids supplied by the endoplasmic reticulum. Here, using biochemical assays and molecular dynamics simulations, authors identify VDAC as a scramblase-type lipid transporter that catalyze lipid entry.

Cryo-EM reveals the molecular architecture of the uroplakin complex within the asymmetric unit membrane (AUM) of the urothelium, helping to correctly identify the crucial E.coli binding site involved in urinary tract infections.

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.

The role of lipid membrane domains in the activation of immune cells remains elusive. New microscopy data on B cell signaling support a mechanism in which lipid membrane domains consolidate upon B cell receptor clustering.