CryoCLEM-guided cryoET of Psd95-GFP knockin mouse tissue and ultra-fresh synaptonerosomes indicate that the postsynaptic density is a not a conserved feature of glutamatergic synapses in the mouse brain.
Piezo proteins induce a curved protein-membrane nanodome with an excess area of about 40 nm2 in tensionless membranes and resist tension-induced flattening with a force constant of about 60 pN/nm.
Structural and computational approaches uncover the molecular basis for dimerization, open-closed conformational transitions, and the dynamic behavior of the human angiotensin-I converting enzyme dimer.
Membrane geometry switches protein condensate organization of postsynaptic density proteins by reducing crowding effects while maintaining specific binding, allowing targeted interactions to dominate over size-based exclusion.
