Assessing Ubiquitylation of Individual Proteins Using Xenopus Extract Systems

Cold Spring Harbor Protocols
Gary S McDowell, Anna Philpott

Abstract

Xenopus extract systems have been used to study ubiquitylation of proteins, and to uncover some of the fundamental processes of the ubiquitylation pathway itself. They provide a simple, quick, and robust method for studying ubiquitylation. In this protocol, methods are provided for studying protein ubiquitylation using Xenopus egg or embryo extracts and in vitro radiolabeled proteins. These methods also enable examination of whether proteins undergo noncanonical ubiquitylation, through modification of the protein by covalent linkage to ubiquitin through residues other than lysine, such as cysteine, serine, and threonine.

References

Jul 12, 2007·The Biochemical Journal·Jonathan M D VosperAnna Philpott
Sep 3, 2010·Biochemical and Biophysical Research Communications·Gary S McDowellAnna Philpott
Mar 6, 2012·Journal of Cell Science·Yelena Kravtsova-Ivantsiv, Aaron Ciechanover
Jun 5, 2013·The International Journal of Biochemistry & Cell Biology·Gary S McDowell, Anna Philpott
Jul 8, 2014·Biochemical and Biophysical Research Communications·Gary S McDowellAnna Philpott
Oct 21, 2016·The International Journal of Developmental Biology·Gary S McDowell, Anna Philpott
Feb 14, 2018·Cold Spring Harbor Protocols·Matthew C Good, Rebecca Heald
May 18, 2018·Cold Spring Harbor Protocols·Gary S McDowell, Anna Philpott

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Citations

Jul 8, 2018·Cold Spring Harbor Protocols·Romain Gibeaux, Rebecca Heald

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