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Cultured dorsal root ganglion neurons lacking the E3 ubiquitin ligase PHR1, which targets the kinase DLK for proteasomal degradation, display high levels of phosphorylation of the MAP kinase JNK (green) in their axons. Huntwork-Rodriguez et al. show that a rapid increase in the abundance of DLK protein occurs after neuronal injury and is important for initiation of downstream signaling events and neuronal apoptosis. Nuclei are labeled red.
Image © 2013 Huntwork-Rodriguez et al.
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In This Issue
In Focus
Crawling cells feel the squeeze
Study finds that cells alter movement style in tight spaces.
People & Ideas
Helder Maiato: Hot (+)TIPs on mitosis
Maiato studies how microtubule plus-end tracking proteins (+TIPs) influence mitosis.
Review
Report
Spindle assembly checkpoint proteins are positioned close to core microtubule attachment sites at kinetochores
Depletion analyses and nanometer-scale mapping of spindle assembly checkpoint proteins reveal how these proteins are integrated within the substructure of the kinetochore.
Article
JNK-mediated phosphorylation of DLK suppresses its ubiquitination to promote neuronal apoptosis
Neuronal injury induces JNK phosphorylation of DLK, which reduces DLK ubiquitination and creates a positive feedback loop to enhance JNK signaling and increase apoptosis.
Adaptation to the spindle checkpoint is regulated by the interplay between Cdc28/Clbs and PP2ACdc55
PP2ACdc55 dephosphorylates APC/CCdc20 to prevent anaphase, an effect that is counteracted by Cdc28/Clbs to allow for spindle checkpoint adaptation.
Centrosome repositioning in T cells is biphasic and driven by microtubule end-on capture-shrinkage
Dynein and microtubule depolymerization drive centrosome repositioning in T cells via microtubule end-on capture-shrinkage operating at the center of the immunological synapse.
Drebrin contains a cryptic F-actin–bundling activity regulated by Cdk5 phosphorylation
Drebrin activity in F-actin bundling and filopodia induction relies on two adjacent F-actin binding sites and a Cdk5 phosphorylation-regulated intramolecular inhibitory interaction.
Distinct signaling mechanisms regulate migration in unconfined versus confined spaces
α4β1 integrin promotes migration of fibroblast-like cells in confined environment by enhancing myosin IIA via Rac1 inhibition, whereas unconfined migration requires Rac1 and myosin IIB.
Correction
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