Bone repair depends on skeletal progenitor cells (SPCs) moving to injured areas and developing into bone-forming cells, but how these cells respond to their surroundings remains unclear. A study published in the International Journal of Oral Science shows that two collagen receptors, β1 integrin and DDR2, work together to regulate SPC migration, proliferation, and differentiation during cranial bone regeneration. The findings reveal a cooperative mechanism that could guide strategies to enhance bone repair.

The textbook view often describes euchromatin, the active part of the genome, as open and accessible. A research team led by Kazuhiro Maeshima has now shown that euchromatin in living human cells forms condensed domains whose local mixing is constrained by cohesin. When cohesin is lost, these domains become more fluid and locally mix without global decompaction, weakening transcriptional insulation.