Nature Structural & Molecular Biology, Published online: 29 September 2025; doi:10.1038/s41594-025-01680-9Issa et al. show that the ciliary small guanosine triphosphatase Arl3 displaces the inhibitory regulator Shulin/DNAAF9 from the outer dynein arm, leading to motor activation.

Linker of nucleo- and cytoskeleton (LINC) complexes reside in the nuclear envelope, the double-membrane surrounding the nucleus, where they establish a physical bridge between nucleus and cytoplasm. L...

Cryo-electron microscopy and biochemical reconstitution analysis reveals that Nde1 enhances Lis1 binding to autoinhibited dynein, promoting formation of a Phi-like–Lis1 intermediate during dynein acti...

Job Title: Associate or Senior Editor, Nature Biomedical Engineering Organization: Nature Portfolio Location: New York, Jersey City, Shanghai or Beijing – Hybrid Working Closing date: August 20, 2025 ...

Title: Associate or Senior Editor, Nature Methods Organization: Nature Portfolio Locations: New York, Jersey City, Shanghai or Beijing Closing Date: August 3, 2025    About Springer Nature Springer Na...

Cell generate forces to maintain normal tissue morphology and function. Cells can also sense and process forces appropriate to their correct tissue context. ...

During mitosis, properly aligned chromosomes stabilise microtubule ends with the help of kinetochores to ensure timely segregation of chromosomes. Microtubule-binding components of the human outer kinetochore, such as Ndc80 and Ska complexes, are present in multiple copies and together bind several microtubule ends, creating a highly multivalent binding interface. Whereas Ndc80:Ndc80 and Ndc80:microtubule binding is crucial for interface stability, Ndc80 alone in absence of Ska is unable to support stable kinetochore-attachments. Using cryoET, we demonstrate that oligomeric Ndc80:Ska assemblies stabilise microtubule ends against shortening by strengthening lateral contacts between tubulin protofilaments at microtubule plus-ends. We further identify a point mutation within the SKA1 microtubule-binding domain that does not affect microtubule-binding of individual Ska molecules, but does abolish Ska:Ska interactions. Finally, we report that oligomerisation of Ska, in a cooperative fashion together with the Ndc80, is necessary to maintain stable microtubule attachments both in vivo and in vitro. ### Competing Interest Statement The authors have declared no competing interest. BBSRC, BB/X014975/1, BB/W019698/1 Wellcome Trust, https://ror.org/029chgv08, 308895/Z/23/Z

Cilia are composed of microtubule doublets, but how they assemble is unclear. Here, the authors show that the brain-specific MAP6d1, found in neuronal primary cilia, assembles doublet microtubules and...

SARS-CoV-2 entry into host cells is mediated by the spike protein, which drives membrane fusion. While cryo-EM reveals stable prefusion and postfusion conformations of the spike, the transient fusion intermediate states during the fusion process remain poorly understood. Here, we design a near-native viral fusion system that recapitulates SARS-CoV-2 entry and use cryo-electron tomography (cryo-ET) to capture fusion intermediates leading to complete fusion. The spike protein undergoes extensive structural rearrangements, progressing through extended, partially folded, and fully folded intermediates prior to fusion-pore formation, a process that depends on protease cleavage and is inhibited by the WS6 S2 antibody. Upon interaction with ACE2 receptor dimer, spikes cluster at membrane interfaces and following S2’ cleavage concurrently transition to postfusion conformations encircling the hemifusion and initial fusion pores in a distinct conical arrangement. S2’ cleavage is indispensable fo

Nature Structural & Molecular Biology, Published online: 23 May 2025; doi:10.1038/s41594-025-01558-wUsing cryo-EM, Kendrick et al. reveal multiple dynein conformations during dynein’s mechanochemical cycle and Lis1 binding that represent intermediate states of dynein’s activation.

Nature Reviews Molecular Cell Biology, Published online: 14 May 2025; doi:10.1038/s41580-025-00854-zThe inner mitochondrial membrane forms cristae, which are crucial for mitochondrial function. This Review explores the protein complexes that regulate cristae dynamics, including remodelling and fusion, and discusses recent structural insights that have increased our understanding of mitochondrial architecture.

Vacancy at Department of Molecular Biology and Genetics - BiRC - Bioinformatics Research Center, Aarhus University

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