Abstract

Ubiquitin-dependent proteolysis is required for cell cycle progression. Here, we demonstrate that the proteasome is activated duringin vivo Xenopusegg activation, induced by treatment with the calcium ionophore A23187. It was found that activation is due to the calcium-induced assembly of the 26 S proteasome from the 20 S proteasome. We propose that proteasome activation is regulated by cell cycle calcium transients, which are controlled upstream by an endogenous cell cycle oscillator that is independent of the cyclin-dependent kinase cycle.

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