Protocol

Ubiquitin Family Modifiers and the Proteasome

Volume 832 of the series Methods in Molecular Biology pp 547-576

Date:

Structural Insights into Functional Modes of Proteins Involved in Ubiquitin Family Pathways

  • Petra HänzelmannAffiliated withRudolf Virchow Center for Experimental Biomedicine, University of Würzburg
  • , Antje SchäferAffiliated withRudolf Virchow Center for Experimental Biomedicine, University of Würzburg
  • , Daniel VöllerAffiliated withRudolf Virchow Center for Experimental Biomedicine, University of Würzburg
  • , Hermann SchindelinAffiliated withRudolf Virchow Center for Experimental Biomedicine, University of Würzburg Email author 

* Final gross prices may vary according to local VAT.

Get Access

Abstract

The conjugation of ubiquitin and related modifiers to selected proteins represents a general mechanism to alter the function of these protein targets, thereby increasing the complexity of the cellular proteome. Ubiquitylation is catalyzed by a hierarchical enzyme cascade consisting of ubiquitin activating, ubiquitin conjugating, and ubiquitin ligating enzymes, and their combined action results in a diverse topology of ubiquitin-linkages on the modified proteins. Counteracting this machinery are various deubiquitylating enzymes while ubiquitin recognition in all its facets is accomplished by numerous ubiquitin-binding elements. In the following chapter, we attempt to provide an overview on enzymes involved in ubiquitylation as well as the removal of ubiquitin and proteins involved in the recognition and binding of ubiquitin from a structural biologist’s perspective.

Key words

Deubiquitylating enzyme (DUB) Ubiquitin Ubiquitin-activating enzyme (E1) Ubiquitin-binding domains Ubiquitin-conjugating enzyme (E2) Ubiquitin ligase (E3) Ubiquitin-like protein