Atomic force microscopy based single-molecule force spectroscopy of smooth muscle myosin light chain kinase strongly indicates the existence of a mechanically triggerable activation pathway analogous to its well-established biochemical regulation pathway via calcium-loaded calmodulin.
The ligand-binding pocket of the Dishevelled PDZ domain can be occupied by Dishevelled's own highly conserved C-terminus, inducing a closed conformation that is ‘opened’ when Wnt signaling stimulates interaction between Frizzled and Dishevelled.
First structural view of a substrate-bound PIKK (PI3K-related-kinase) by cryo-EM explains phosphorylation specificity toward a short amino-acid motif shared across the PIKK family and rationalizes PIKK auto-inhibition by regulatory domain.
Single molecule FISH analysis defines the behavior of centromere-derived alpha-satellite transcripts in intact human cells and reveals a critical role for centromere-nucleolar contacts in repressing alpha-satellite transcription.
Casein kinase 1G2 interacts with and inhibits the activation of receptor-interacting kinase 3, RIP3, in response to TNF and toll-like receptor family members and attenuates its necroptosis signaling activity.