The crystal structure of a mammalian protein kinase G reveals contacts between the regulatory and catalytic domains, indicates how cGMP binding alters domain conformations and thus domain:domain interactions, and informs a model for enzyme auto-inhibition and cooperative activation.

A minimal subset of two to three residues in cyclic nucleotide binding (CNB) domains controls nucleoside vs. cyclic nucleotide specificity, repurposing PKA of certain pathogens for novel nucleoside signaling pathways or sensing.

Alms1a is a centrosomal protein that exhibits asymmetric localization between mother and daughter centrosomes in asymmetrically dividing stem cells in Drosophila testis, controlling centriole duplication.

Longevity in C. elegans is influenced not only by insulin/IGF-1 signalling, but also by CAMKII and calcineurin, acting on the same target, the transcription factor DAF-16.

Cryo-electron microscopy reconstructions of two microtubule-bound transport kinesins at 7 Å resolution reveal how microtubule track binding stimulates ADP release, primes the active site for ATP binding and enables force generation.

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.

MKLP2 is a divergent molecular motor that has structurally evolved to bind its microtubule track and use the energy of ATP in distinct ways, tuned according to its function in cell division.

Time-resolved phosphoproteomics and thermal proteome profiling reveal the Ca²⁺-responsive proteome of the model apicomplexan Taxoplasma gondii, identifying PP1 as a Ca²⁺-responsive enzyme that regulates Ca²⁺ uptake to promote parasite motility.

The protein UNC-8 is a neuronal activity sensor that triggers the elimination of synapses during development of the nervous system.

The motor protein kinesin utilizes its fuel molecule by active and concerted motions of its subdomains, while it rapidly interacts with the microtubule track by forming a wet and dynamic interface.