Identification and inhibition of the Cyclin D Rb-docking interface that drives cell division

The paper investigates how D-type cyclins (Cyclin D with CDK4/6) engage their substrates during the cell division cycle, focusing on how cyclin D can dock substrates when its hydrophobic patch is already occupied by assembly factors p21 and p27. Using mechanistic and biochemical approaches, the authors show that D-type cyclins use a specific A2’ helix interface to dock the retinoblastoma protein Rb, and they identify the cyclin D–A2’ helix interface as unique among cyclins. They report that mutating this interface slows proliferation. The paper frames this as a cyclin D–substrate docking mechanism that could be targeted, while the main limitation is that the functional evidence for inhibition and therapeutic potential is based on interface perturbation rather than demonstrating in vivo efficacy. This paper does not explicitly discuss endometriosis or adenomyosis; it was included in the corpus via a keyword match in the upstream search index.

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