GPR161 structure uncovers the redundant role of sterol-regulated ciliary cAMP signaling in the Hedgehog pathway.

The orphan G protein-coupled receptor (GPCR) GPR161 plays a central role in development by suppressing Hedgehog signaling. The fundamental basis of how GPR161 is activated remains unclear. Here, we determined a cryogenic-electron microscopy structure of active human GPR161 bound to heterotrimeric G.

GPR161 structure uncovers the redundant role of sterol-regulated ciliary cAMP signaling in the Hedgehog pathway.

The orphan G protein-coupled receptor (GPCR) GPR161 is enriched in primary cilia, where it plays a central role in suppressing Hedgehog signaling. GPR161 mutations lead to developmental defects and cancers. The fundamental basis of how GPR161 is activated, including potential endogenous activators and pathway-relevant signal transducers, remains unclear.

Community waterborne outbreak linked to a firefighting response during the COVID-19 emergency.

Background: On 6 March 2020, a big fire in a village forced the firefighters to draw water simultaneously from many sources, including the Adige river. From 9 March, an increasing number of inhabitants reported gastrointestinal symptoms. We describe the outbreak and the challenges linked to the concurrent COVID-19 spread.

Generation of an hiPSC-1 knock-in line expressing TY1-tagged MNX1-protein together with mScarlet.

MNX1 encodes a homeobox transcription factor with conserved embryonic requirements in spinal motor neuron formation and pancreatic beta-cell differentiation. Mutations in MNX1 are associated with dominantly inherited Currarino syndrome and neonatal diabetes. To better understand embryonic MNX1 functions we generated an hiPSC-1 knock-in line heterozygously expressing MNX1 C-terminally tagged with 2xTY1 together with a T2A-separated red fluorescent reporter mScarlet.