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The measurement of ubiquitin and ubiquitinated proteins
Author(s) -
Mimnaugh Edward G.,
Bonvini Paolo,
Neckers Len
Publication year - 1999
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/(sici)1522-2683(19990201)20:2<418::aid-elps418>3.0.co;2-n
Subject(s) - ubiquitin , f box protein , microbiology and biotechnology , phosphorylation , signal transduction , computational biology , function (biology) , protein degradation , transcription factor , biology , ubiquitin ligase , chemistry , gene , biochemistry
Ubiquitination of key cellular proteins involved in signal transduction, gene transcription and cell‐cycle regulation usually condemns those proteins to proteasomal or lysosomal degradation. Additionally, cycles of reversible ubiquitination regulate the function of certain proteins in a manner analogous to phosphorylation. In this short review we describe the current methodology for measuring ubiquitin and ubiquitination, provide examples which illustrate how various techniques have been used to study protein ubiquination, alert the readers of pitfalls to avoid, and offer guidelines to investigators newly interested in this novel post‐translational protein modification.