A phosphorylation-driven ubiquitination switch for cell-cycle control.

J Wade Harper

doi:10.1016/s0962-8924(01)02238-3

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A phosphorylation-driven ubiquitination switch for cell-cycle control.

J Wade Harper

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Abstract

Cellular changes in state can be dictated by complex all-or-nothing switches built from ultrasensitive protein kinase cascades, positive-feedback loops and other mechanisms. Recent work has established that phosphorylation-driven protein destruction through the SCF ubiquitin-ligase pathway can also occur in a switch-like manner. In this context, multiple phosphorylation events are used to set a threshold for substrate targeting, thereby providing a framework for understanding the inter-relationship between protein phosphorylation and ubiquitin-mediated proteolysis.

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CDC28 Protein Kinase, S cerevisiae Cell Cycle Proteins Cyclin-Dependent Kinase Inhibitor Proteins Enzyme Inhibitors Feedback, Physiological Fungal Proteins Phosphorylation Saccharomyces cerevisiae Proteins Ubiquitins Yeasts News Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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J Wade Harper. 2002. A phosphorylation-driven ubiquitination switch for cell-cycle control.. https://doi.org/10.1016/s0962-8924(01)02238-3

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