Microglia as hunters or gatherers of brain synapses.

Over a decade ago, it was discovered that microglia, the brain's immune cells, engulf synaptic material in a process named microglial pruning. This term suggests that microglia actively sculpt brain circuits by tagging and phagocytosing unwanted synapses. However, live imaging studies have yet to demonstrate how microglial synapse elimination occurs.

Cracking the membrane lipid code.

Why has nature acquired such a huge lipid repertoire? Although it would be theoretically possible to make a lipid bilayer fulfilling barrier functions with only one glycerophospholipid, there are diverse and numerous different lipid species. Lipids are heterogeneously distributed across the evolutionary tree with lipidomes evolving in parallel to organismal complexity. Moreover, lipids are different between organs and tissues and even within the same cell, different organelles have characteristic lipid signatures.

Ultrastructure of COPII vesicle formation in yeast characterized by correlative light and electron microscopy.

Traffic of proteins out of the endoplasmic reticulum (ER) is driven by the COPII coat, a layered protein scaffold that mediates the capture of cargo proteins and the remodeling of the ER membrane into spherical vesicular carriers. Although the components of this machinery have been genetically defined, and the mechanisms of coat assembly extensively explored in vitro, understanding the physical mechanisms of membrane remodeling in cells remains a challenge. Here we use correlative light and electron microscopy (CLEM) to visualize the nanoscale ultrastructure of membrane remodeling at ER exit sites (ERES) in yeast cells.

Cargo crowding contributes to sorting stringency in COPII vesicles.

Accurate maintenance of organelle identity in the secretory pathway relies on retention and retrieval of resident proteins. In the endoplasmic reticulum (ER), secretory proteins are packaged into COPII vesicles that largely exclude ER residents and misfolded proteins by mechanisms that remain unresolved. Here we combined biochemistry and genetics with correlative light and electron microscopy (CLEM) to explore how selectivity is achieved.

Lysophospholipids Facilitate COPII Vesicle Formation.

Coat protein complex II (COPII) proteins form vesicles from the endoplasmic reticulum to export cargo molecules to the Golgi apparatus. Among the many proteins involved in this process, Sec12 is a key regulator, functioning as the guanosine diphosphate (GDP) exchange factor for Sar1p, the small guanosine triphosphatase (GTPase) that initiates COPII assembly. Here we show that overexpression of phospholipase B3 in the thermosensitive sec12-4 mutant partially restores growth and protein transport at non-permissive temperatures.

Multi-centre audit of VMAT planning and pre-treatment verification.

Background And Purpose: We performed a multi-centre intercomparison of VMAT dose planning and pre-treatment verification. The aims were to analyse the dose plans in terms of dosimetric quality and deliverability, and to validate whether in-house pre-treatment verification results agreed with those of an external audit.

Materials And Methods: The nine participating centres encompassed different machines, equipment, and methodologies.

Hormones and silk. Gay men in the Spanish film comedies of the transition to democracy (1976-1981).

This article studies the representation of gay men in Spanish comedies of the 1970s. It analyzes how cinema used the stereotypical image of gay men projected by the dictatorship and how, once it ended, this image endured in the comedy genre. It introduces film theories on the construction of humor taken from relevant authors, such as Jordan, Charney, Voitylla, and Petri.

Protein O-mannosyltransferases participate in ER protein quality control.

In eukaryotic cells, proteins enter the secretory pathway at the endoplasmic reticulum (ER) as linear polypeptides and fold after translocation across or insertion into the membrane. If correct folding fails, many proteins are O-mannosylated inside the ER by an O-mannosyltransferase, the Pmt1p-Pmt2p complex. The consequences of this modification are controversial and the cellular role of the Pmt1p-Pmt2p complex in this respect is unclear.