Building on previous work (Froelich et al., 2014), we present the X-ray crystal structure of an active MCM hexamer, which suggests a mechanism for MCM regulation and demonstrates a key interaction between the major domains.
The crystal structure of the MCM helicase bound to single-stranded DNA reveals a binding motif that is critical for cell viability, helicase activation and DNA replication.
The role of the Frazzled chemoattractant receptor is to triggers migration initiation as part of the glial developmental program induced by the Glide/Gcm transcription factor.
The archaeal MCM helicase can load in multiple orientations on DNA but translocation proceeds with a leading N-terminal domain, which affects double hexamer activation at origins of replication.
Cell-cell junctions and the actin cytoskeleton are key players in the organisation and patterning of the extracellular matrix (ECM) on the apical side of tracheal cells.
Soluble fragments cleaved from the N-terminus of PC-1 activate the PC-1/PC-2 heteromeric polycystin channel, describing for the first time that the N-terminus itself is an endogenous ligand.
During early cortical development, microRNA-128 regulates the homeostasis of neural stem cells by targeting PCM1, a protein that is critical for cell division.
Genetic, biochemistry and modeling approaches reveal elements of a Turing-type reaction-diffusion system to control pattern formation in differentiating cyanobacterial filaments.
