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.
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 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.
The structure of the photosystem I (PSI) complex from Synechocystis is determined, and reaction center subunits engineered to resemble a viral PSI are found to promote promiscuous electron acceptor properties.
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.
Ciliogenesis is regulated by a certain group of centriolar satellite proteins, among which an E3 ligase is tethered by PCM1 to maintain the normal level of pro-ciliogenic protein on centrioles.
During early cortical development, microRNA-128 regulates the homeostasis of neural stem cells by targeting PCM1, a protein that is critical for cell division.
The centromeric protein CENP-T assembles the microtubule-binding interface of kinetochores through direct recruitment of two Ndc80 complexes and indirect recruitment of a third one through the Mis12 complex.
