ESCRT-III heteropolymers utilize non-specific lateral electrostatic interactions to recognize one another, which may enable the polymers to slide along one another and adapt to different curvatures.
Hans Moldenhauer, Ignacio Díaz-Franulic ... David Naranjo
Detection of unbinding transitional states in the charybdotoxin first-order dissociation from a Kv-channel reveals that the bound neurotoxin wobbles, suggesting diverse intermediates and dissociation pathways in this protein–protein interaction.
Ben F Brian IV, Adrienne S Jolicoeur ... Tanya S Freedman
The ubiquitin ligase c-Cbl preferentially targets unique-region phosphorylated LynA for rapid degradation, regulating its expression and differentially tuning signaling responsiveness in macrophages and mast cells.
Anita Santana-Sanchez, Daniel Solymosi ... Yagut Allahverdiyeva
In vivo evidence is provided indicating that Flv2/Flv4, together with Flv1/Flv3, mediate O2 photoreduction downstream of PSI in a highly coordinated manner.
Samantha Del Borrello, Margot Lautens ... Andrew G Fraser
Parasitic helminths infect over a billion humans and use unusual anaerobic metabolism that needs a rare electron carrier, Rhodoquinone (RQ), whose synthesis requires the kynurenine pathway of tryptophan degradation.
N-chlorination, a reversible, oxidative modification, turns plasma proteins into holdase-like chaperones, potent activators of immune cells and pro-survival factors for phagocytic immune cells.
CMG helicase translocates with force while encircling duplex DNA, enabling two opposing CMG complexes at an origin to melt the duplex and switch to encircling separate single strands.
The structure of a light-sensitive G protein-coupled receptor in complex with a Gi-protein heterotrimer provides a structural foundation for the role of the receptor C-terminal tail in scaffolding and signaling.
The autophagy protein ATG2A tethers membranes and transfers lipids between them, suggesting that autophagosome membranes grow upon the acquisition of lipids from the ER through the ATG2A bridge.