eMags is an engineered photodimerizer pair for optogenetic modulation in mammalian cells that is especially suited for the manipulation of intracellular processes occurring in small volumes or subcellular organelles.

Components of the nuclear pore complex share structural and functional features with soluble nuclear transport receptors, which suggests that there may be an evolutionary relationship between these two types of protein.

Cryo-EM structures of rotary V-ATPase reveal the ON-OFF switching mechanism of H⁺ translocation in the V_o membrane domain.

The model organism Tetrahymena thermopile carries two nuclei with distinct genomes: an unrearranged germline genome with five chromosomes, and a somatic genome reduced in size by a third and with 181 chromosomes.

Interconnected RNA processing mechanisms ensure the fidelity of non-conventional mRNA splicing during the unfolded protein response.

Molecular structure of mitochondrial complex I from Drosophila melanogaster reveals a structural element not seen in other organisms to date that may regulate the transition between an off-pathway resting state and the active state of the complex.

The dynein light intermediate chain is a member of the G protein superfamily and links the motor to several intracellular cargo adaptors.

It is technically difficult to identify transport proteins, but here a method is presented that exploits the principle that they are stabilized in detergent solution when they bind their substrate.

Protein disaggregases employ two mechanically-linked ATPase rings that are under steric control by a wrapped-around coiled-coil belt.

Exploring natural Hsp104 variation reveals unexpected tuning of a passive activity that inhibits aggregation of specific substrates to selectively counter TDP-43 or alpha-synuclein proteotoxicity connected to neurodegenerative disease.