A cryo-electron microscopy study of the human CLC-1 chloride ion channel reveals the structural basis of why some CLC proteins function as passive chloride channels whereas others function as an active proton-chloride antiporters.
A multidisciplinary platform featured by patient-derived RPEs is established to study the disease-causing mechanisms of BEST1 mutations, and demonstrates gene-supplemented rescue of the mutation-caused deficiency in Ca2+-dependent Cl- current in human RPE.
The characterization of a previously unidentified “outward-facing open” conformational state provides a new framework for understanding the CLC transport mechanism.
Clarinet, a novel C. elegans active zone protein with homology to vertebrate Piccolo and Rim, uses its different isoforms for diverse functions, including synaptic vesicle clustering, vesicle release and synaptogenesis.
The maize CLAVATA receptor, FEA2, functions in the perception of two different ligands, and remarkably that signaling from these different inputs is differentiated by the receptor interacting with two different downstream components.
Measuring the equilibrium dimerization of a polytopic membrane protein in lipid bilayers forms the basis of a new system for studying the physical forces that stabilize membrane protein association in membranes.
The near-atomic cryoEM pore complex structure of pneumolysin, the main virulence factor of Streptococcus pneumoniae, shows how the individual domains rearrange during the pore formation.
TMEM206 proteins are identified as constituting the pore of the widely expressed acid-activated chloride channel PAORAC/ASOR, which is important in acid toxicity.
Head-to-head interactions of regulatory coiled-coil domains control activity of the central bacterial AAA+ protein ClpC by promoting formation of a reversible resting state.
