Plexin controls the spatial distribution of synapses by locally inhibiting Rap2 small GTPase activity along the axon, and a Rap2 effector, TNIK, which also plays a key role in inhibiting synapse number.
Charles F Ericson, Fabian Eisenstein ... Nicholas J Shikuma
Bacteria produce a syringe-like structure, loaded with a single protein within the lumen of its needle-like tube, that is sufficient for stimulating animal metamorphosis.
The emerging importance of interorganellar communication is demonstrated by documentation of a feedback loop wherein peroxisome-generated metabolites affect mitochondrial ATP production and peroxisomal functions via signaling pathways requiring transmission of signals also through the cytosol and the nucleus.
Vishnu Muraleedharan Saraswathy, Akshai Janardhana Kurup ... Maximilian Fürthauer
Mindbomb1 acts independently of it well-known role in Notch signalling to control the endocytic internalization of the Wnt co-receptor Ryk and thereby modulate the activity of the Planar Cell Polarity pathway that governs morphogenetic movements during embryonic development.
Tie-Zhong Cui, Tabitha A Peterson, Christopher G Burd
The CDC25 family protein phosphatase Mih1 promotes downregulation of cell surface proteins in budding yeast by dephosphorylating a subunit of the retromer complex, which mediates plasma membrane recycling.
The convergent evolution of yeast Mim1/2 and trypanosomal pATOM36 enable the first demonstration of reciprocal functional rescue of two evolutionary unrelated mitochondrial biogenesis complexes belonging to two different eukaryotic supergroups.
A gradient of Mib1-Dll4 within multinucleated muscle fibers maintains a continuum of metastable states within the muscle stem cell pool during tissue homeostasis.
Newly forming descending pathways are arranged to function in parallel to existing ones and contribute to increasingly sophisticated locomotor behaviors that emerge postnatally with suitable connectivity patterns and biophysical properties.
Anna Caballe, Dawn M Wenzel ... Juan Martin-Serrano
ULK3 is a kinase in the abscission checkpoint that temporarily inactivates ESCRT-III proteins via phosphorylation, which is required to delay cytokinesis in response to defects in mitosis.