Harry H. Low

TL;DR: In this review, the basis for an emerging consensus on how dynamin functions is presented, and three properties of dynamin are strongly supported by experimental data: first, dynamin oligomerizes into a helical polymer; second, dynamIn oligomer constricts in the presence of GTP; and third, dynam in catalyzes membrane fission upon GTP hydrolysis.

TL;DR: All three opioid receptors are involved in the response to inflammation and that they may play different roles in this pathological state, suggesting the coexistence of MOR, DOR, and KOR in at least some primary sensory neurons provides a substrate for functional interactions between these receptors.

TL;DR: This work uses electron microscopy to reconstruct the type IV secretion system encoded by the Escherichia coli R388 conjugative plasmid and shows a secretion system with markedly different architecture, and consequently mechanism, to other known bacterial secretion systems.

TL;DR: Structural and mechanistic insight is provided and compelling similarity is shown between a cyanobacterial and chloroplast DLP that, given the endosymbiotic ancestry of chloroplasts, questions the evolutionary origins of dynamins.

TL;DR: Nucleotide hydrolysis seems to be coupled to polymer disassembly and dissociation from lipid, rather than membrane restructuring, so observed structural similarities with rat dynamin 1 suggest that the results have broad implication for other dynamin family members.