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Significance Attachment of the small protein ubiquitin to other proteins, a process called “ubiquitylation,” triggers protein degradation. The Cullin and signalosome protein families cooperatively mediate this process, but how they are regulated has been obscure. We show that an inositol polyphosphate with seven phosphates, hence designated IP7, is critical. Under basal conditions, the enzyme that generates IP7 is bound to the Cullin/signalosome complex, which is thereby maintained in an inactive state. Stressful stimuli, such as UV radiation, stimulate the enzyme to form IP7, which dissociates the complex, leading to activation of the Cullins with attendant ubiquitylation and degradation of target proteins. This process may play a key role in how cells respond to environmental stressors.

Inositol hexakisphosphate kinase-1 mediates assembly/disassembly of the CRL4–signalosome complex to regulate DNA repair and cell death