A prominent model for the structural organisation of the Tat (twin-arginine translocase) protein transport system fails live cell tests.

Evolutionary bioinformatics and experimentation are applied to the components of the Tat protein transport system to elucidate the structure of the membrane-bound receptor complex and to deduce a molecular description for its substrate-triggered activation.

Bioinformatics and experimental approaches identify families of membrane proteins requiring the co-ordinated action of the Sec pathway and Tat pathways for their integration and define features of the polypeptides that mediate interaction with these pathways.

Cationic cell-penetrating peptides (CPPs) enter cells through ~2 (–5)-nm-wide water pores induced by the strong negative plasma membrane potential that CPPs and the activity of potassium channels generate.

The time it takes to secrete a protein is dominated by diffusion of positively charged arginines through the channel across the membrane, but lysines avoid this problem as they are neutralised before transport.

A novel DUB-regulated mechanism controls polarized axon growth and guidance.

D-serine has a major role in the regulation of NMDA receptors not only contributing to its activation as the receptors co-agonist, but also by regulating specifically GluN2B-NMDA receptor trafficking and synaptic content at developing hippocampal synapses.

A peripheral sense-organ glia actively engulfs fragments of a sensory neuron ending to modify neuron shape and associated animal sensory behavior in Caenorhabditis elegans..

Proteins for bacterial flagella biogenesis contain two discrete export signals, recognised sequentially by the flagellar Type III Secretion System to facilitate initial docking and subsequent opening of the export gate.

The endo-lysosomal system plays a positive essential role in the initiation of the cell cycle in yeast.