Ion occupancy of the selectivity filter controls opening of a cytoplasmic gate in the K channel TALK-2.

Two-pore domain K (K) channel activity was previously thought to be controlled primarily via a selectivity filter (SF) gate. However, recent crystal structures of TASK-1 and TASK-2 revealed a lower gate at the cytoplasmic pore entrance. Here, we report functional evidence of such a lower gate in the K channel K2P17.

Toxic Metamorphosis-How Changes from Lysosomal to Cytosolic pH Modify the Alpha-Synuclein Aggregation Pattern.

Alpha-synuclein (aSyn) is a cytosolic, aggregation-prone protein that is associated with neurodegenerative disorders like Parkinson's disease. Interestingly, the protein can appear in different conformations, including monomeric and oligomeric forms as well as amyloid fibrils. Its individual structural constituents seem to be dependent on various factors and the composition of the respective cellular surroundings.