A structure-based model of the chromosomal cohesin complex, accompanied by molecular-mechanistic simulations, explains cohesin's key role in topologically entrapping DNA, as well as its ability to alternatively extrude DNA loops.
Absolute quantification of cohesin, CTCF, NIPBL, WAPL and sororin in HeLa cells implies that some genomic cohesin and CTCF enrichment sites are unoccupied at any one time.
Hypersensitivity of cohesin-deficient cells to Wnt signaling is concomitant with beta catenin stabilization and offers promise that Wnt agonists could be therapeutically effective in cohesin mutant cancers.
Rigorous biochemical and structural analyses reveal the precise topology of cohesin's association with DNA and suggest a mechanism for how DNA is transported inside the ring.
Cohesin adopts a flexible butterfly conformation in vivo and forms spatial and temporal regulated ordered clusters to maintain cohesion and condensation.
In G1 cells, Scc2 loads and maintains cohesin on chromosomes by counteracting a Wapl-independent releasing activity, which is neutralized in S phase by CDK1.
Systematic analyses of DNA replication machinery components in human cells reveal a requirement of MCM-dependent de novo loading or mobilization of cohesin at replication forks in establishing sister-chromatid cohesion.
High-resolution mapping of cohesin-dependent chromatin loops in the genome of budding yeast reveals evolutionarily conserved features for loop formation and cohesin residency as a determinant of loop positioning.
Sister chromatid cohesion is established during replication by two independent pathways operating in parallel, one converts chromosomal cohesin into cohesive structures while the other loads cohesin onto nascent DNAs.
