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In vitro reconstitution reveals how a system of molecules works together to transport the motor protein dynein to the start of its track.

The combinatorial assembly of different adaptor complexes is a mechanism that dynein uses to interact with multiple cargos.

Structural and functional studies reveal how a ubiquitous regulator of dynein keeps the microtubule-based motor in a persistent track-bound state.

New cryoEM structures reveal how small bacteriophage proteins suppress bacterial immunity.

A single-cell assay reveals that the genetic rewiring that underlies PARP inhibitor resistance drives altered DNA double-strand break end resection pathway choice.

The membrane proteins Reck and Gpr124 are integral components of a novel Wnt7a/Wnt7b-specific signaling complex, and there is a distinctive requirement for Wnt/β-catenin signaling in tip cells during angiogenesis in the central nervous system.

Phase separated DNA-free stored forms of RecA dissolve in response to DNA damage to make RecA available for repair and recombination reactions as part of the bacterial (Escherichia coli) SOS response.

A new optical tweezers assay sheds light on the mechanism of cooperation and force generation by the subunits of RecBCD, critical for the repair of double strand breaks in bacteria.

Structures of human cytoplasmic dynein-1 bound to its regulator LIS1 reveal the interfaces involved in forming the complex and provide a context for disease-linked mutations.

Molecular dissection of Frizzled, Reck, and Wnt7a provides critical insight into the long-standing question of ligand-receptor specificity in the field of Wnt signaling.