Abstract:
:Regulated proteolysis plays important roles in cell biology and pathological conditions. A crosstalk exists between apoptosis and the ubiquitin-proteasome system, two pathways responsible for regulated proteolysis executed by different proteases. To investigate whether the apoptotic process also affects the 20S proteasome, we performed three independent SILAC-based quantitative proteome approaches: 1-DE/MALDI-MS, small 2-DE/MALDI-MS and large 2-DE/nano-LC-ESI-MS. Taking the results of all experiments together, no quantitative changes were observed for the α- and β-subunits of the 20S proteasome except for subunit α7. This protein was identified in two protein spots with a down-regulation of the more acidic protein species (α7a) and up-regulation of the more basic protein species (α7b) during apoptosis. The difference in these two α7 protein species could be attributed to oxidation of cysteine-41 to cysteine sulfonic acid and phosphorylation at serine-250 near the C terminus in α7a, whereas these modifications were missing in α7b. These results pointed to the biological significance of posttranslational modifications of proteasome subunit α7 after induction of apoptosis.
journal_name
Amino Acidsjournal_title
Amino acidsauthors
Schmidt F,Dahlmann B,Hustoft HK,Koehler CJ,Strozynski M,Kloss A,Zimny-Arndt U,Jungblut PR,Thiede Bdoi
10.1007/s00726-010-0575-6subject
Has Abstractpub_date
2011-07-01 00:00:00pages
351-61issue
2eissn
0939-4451issn
1438-2199journal_volume
41pub_type
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