Rnf2 (Ring1b) deficiency causes gastrulation arrest and cell cycle inhibition.

The highly homologous Rnf2 (Ring1b) and Ring1 (Ring1a) proteins were identified as in vivo interactors of the Polycomb Group (PcG) protein Bmi1. Functional ablation of Rnf2 results in gastrulation arrest, in contrast to relatively mild phenotypes in most other PcG gene null mutants belonging to the same functional group, among which is Ring1. Developmental defects occur in both embryonic and extraembryonic tissues during gastrulation.

Type I PIPkinases interact with and are regulated by the retinoblastoma susceptibility gene product-pRB.

Inositide signaling at the plasma membrane has been implicated in the regulation of numerous cellular processes including cytoskeletal dynamics, vesicle trafficking, and gene transcription. Studies have also shown that a distinct inositide pathway exists in nuclei, where it may regulate nuclear processes such as mRNA export, cell cycle progression, gene transcription, and DNA repair. We previously demonstrated that nuclear PtdIns(4,5)P(2) synthesis is stimulated during progression from G1 through S phase, although mechanistic details of how cell cycle progression impinges on the regulation of nuclear inositides is unknown.