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The C2-domain of cytoplasmic phospholipase A₂α is structurally designed to target PC-rich membrane regions to increase the enzymatic efficiency of the catalytic domain, which prefers PCs with polyunsaturated acyl chains.

Ligand-induced two-fold symmetric arrangement in TRPV2 is observed in the native-like nanodisc-reconstituted condition using cryo-electron microscopy.

C-terminal domain of thermoTRPV channels regulates channel gating at the cytoplasmic interface through a switch-like process.

Structural and biochemical analysis reveals that two intrinsically disordered domains of the transcription factor FoxM1 co-fold to form an autoinhibited conformation, which is disrupted by a specific activating phosphorylation event.

Force generation by kinesin motor proteins requires formation of both a 2-stranded cover-neck bundle and an asparagine-based latch for transport of membrane-bound cargoes in cells.

Animal RanBP1 nuclear export and cargo dissociation mechanisms are surprisingly different from yeast, due to mutations of critical residues, leading to greater nuclear transport efficiency and higher energy cost.

Age-dependent protein aggregation closely resembles protein aggregation associated with neurodegenerative diseases and other amyloidoses, and initiates early functional decline in different tissues.

Transient DNA interactions by DNA-binding proteins are utilized by herpes simple virus as an alternative route to generate membraneless compartments in the nucleus without invoking phase separation.

During CRISPR adaptation, Cas4 forms a ternary complex with the Cas1-Cas2 spacer integration complex, an interaction that coordinates substrate hand-off following precise, PAM-dependent prespacer processing prior to integration.

Native state dynamics of mouse prion protein were measured, and these motions were shown to be having a role in initiation of aggregation.