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Ubiquitin Family Modifiers and the Proteasome

Volume 832 of the series Methods in Molecular Biology pp 163-171

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Role of UbL Family Modifiers and Their Binding Proteins in Cell Signaling

  • Sjoerd J. L. van WijkAffiliated withFrankfurt Institute for Molecular Life Sciences and Institute of Biochemistry II, Goethe University School of Medicine
  • , Magda BienkoAffiliated withFrankfurt Institute for Molecular Life Sciences and Institute of Biochemistry II, Goethe University School of MedicineDepartments of Physics and of Biology, Massachusetts Institute of Technology
  • , Ivan DikicAffiliated withFrankfurt Institute for Molecular Life Sciences and Institute of Biochemistry II, Goethe University School of Medicine Email author 

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Abstract

The versatile function of ubiquitin (Ub) is powerfully illustrated by its appearance in multiple forms and shapes, like polymeric ubiquitin chains. These chains, when recognized by specific ubiquitin-binding domains (UBDs), give rise to extraordinary complex signaling networks that regulate virtually every cellular function. At the heart of our understanding of this complexity is the evolution and adaptation of technologies and methods to analyze ubiquitin biochemistry, e.g., covalent Ub–substrate conjugates as well as transient Ub–UBD interactions. Here, we describe seminal developments in those methodologies that have paved the way to our understanding of the diversity of Ub signals as well as their recognition and interpretation by UBD-containing proteins.

Key words

Polyubiquitin chains Ubiquitin-binding domains Linkage-specific antibodies Mass spectrometry SILAC AQUA