Sumoylation as a Signal for Polyubiquitylation and Proteasomal Degradation

Chapter Details

Pub Date: 11 Aug 2010
Pages: 21
Chapter Category: Adhesion Molecules
Taken from the Book: Conjugation and Deconjugation of Ubiquitin Family Modifiers
Book Series: Special Books
Edited by: Marcus Groettrup

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Sumoylation as a Signal for Polyubiquitylation and Proteasomal Degradation

Maria Miteva, Kirstin Keusekotten, Kay Hofmann, Gerrit J.K. Praefcke and R. Jürgen Dohmen

About this Chapter

The small ubiquitin‑related modifier (SUMO) is a versatile cellular tool to modulate a protein’s function. SUMO modification is a reversible process analogous to ubiquitylation. The consecutive actions of E1, E2 and E3 enzymes catalyze the attachment of SUMO to target proteins, while deconjugation is promoted by SUMO specific proteases. Contrary to the long‑standing assumption that SUMO has no role in proteolytic targeting and rather acts as an antagonist of ubiquitin in some cases, it has recently been discovered that sumoylation itself can function as a secondary signal mediating ubiquitin‑dependent degradation by the proteasome. The discovery of a novel family of RING finger ubiquitin ligases bearing SUMO interaction motifs implicated the ubiquitin system in the control of SUMO modified proteins. SUMO modification as a signal for degradation is conserved in eukaryotes and ubiquitin ligases that specifically recognize SUMO‑modified proteins have been discovered in species ranging from yeasts to humans. This review summarizes what is known about these ligases and their role in controlling sumoylated proteins.

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