Abstract:
:Ubiquitin is an essential, highly-conserved small regulatory protein in eukaryotic cells. It covalently modifies a wide variety of targeted proteins in the forms of monomer and polymers, altering the conformation and binding properties of the proteins and thus regulating proteasomal delivery, protein activities and localization. Mass spectrometry has emerged as an indispensable tool for in-depth characterization of protein ubiquitination. Ubiquitinated proteins in cell lysates are usually enriched by affinity chromatography and subsequently analyzed by mass spectrometry for identification and quantification. Ubiquitin-conjugated amino acid residues can be determined by unique mass shift caused by the modification. Moreover, the complex structure of polyubiquitin chains on substrates can be dissected by bottom-up and middle-down mass spectrometric approaches, revealing potential novel functions of polyubiquitin linkages. Here I review the advances and caveats of these strategies, emphasizing caution in the validation of ubiquitinated proteins and in the interpretation of raw data.
journal_name
BMB Repjournal_title
BMB reportsauthors
Peng Jdoi
10.5483/bmbrep.2008.41.3.177subject
Has Abstractpub_date
2008-03-31 00:00:00pages
177-83issue
3eissn
1976-6696issn
1976-670Xjournal_volume
41pub_type
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