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Article
SNARE chaperone Sly1 directly mediates close-range vesicle tethering
SM proteins catalyze accurate assembly of SNARE prefusion complexes. The SM Sly1 operates at early secretory organelles. Duan et al. show that Sly1 directly contacts incoming vesicle membranes. This both activates Sly1, and tethers vesicle and target membranes at close range to promote SNARE-mediated fusion.
SM protein Sly1 and a SNARE Habc domain promote membrane fusion through multiple mechanisms
SM proteins are essential SNARE cofactors for membrane fusion. The ER–Golgi SM, Sly1, has several different activities reported to promote fusion. Here, Duan et al. test each function in parallel genetic and biochemical reconstitution experiments. The results show that all of them are important for efficient fusion. A working model for the order of events is presented.
WW domains form a folded type of nuclear localization signal to guide YAP1 nuclear import
Yang et al. report a novel class of nuclear localization signals served by the family of WW domains, termed WW-NLS, to elucidate the nuclear import mechanism of YAP1 and thus propose a new strategy to interfere with YAP1-dependent cancer progression.
Fascin-induced bundling protects actin filaments from disassembly by cofilin
Chikireddy et al. investigate how crosslinker fascin delays cofilin-induced actin filament disassembly. Fascin hampers the initial formation of cofilin clusters, triggering interfilament cooperativity, which favors subsequent cluster formation but does not enhance severing per cluster. This study deciphers the role of crosslinkers in actin turnover.
N-cadherin dynamically regulates pediatric glioma cell migration in complex environments
Pediatric gliomas invade the brain by migrating between nerve cells or exploiting extracellular matrix along blood vessels. This research reveals crosstalk between YAP1/TAZ signaling and N-cadherin that regulates leader–follower cell phenotypes and migration efficiency in neural and extracellular matrix environments.