Abstract
Alternative translation initiation is a mechanism whereby functionally altered proteins are produced from a single mRNA. Internal initiation of translation generates N-terminally truncated protein isoforms, but such isoforms observed in immunoblot analysis are often overlooked or dismissed as degradation products. We identified an N-terminally truncated isoform of human Dok-1 with N-terminal acetylation as seen in the wild-type. This Dok-1 isoform exhibited distinct perinuclear localization whereas the wild-type protein was distributed throughout the cytoplasm. Targeted analysis of blocked N-terminal peptides provides rapid identification of protein isoforms and could be widely applied for the general evaluation of perplexing immunoblot bands.
Original language | English (US) |
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Pages (from-to) | 2441-2445 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 583 |
Issue number | 14 |
DOIs | |
State | Published - Jul 21 2009 |
Keywords
- Alternative translation initiation
- Dok-1 protein isoform
- N-acetylation
- N-terminal truncation
- Targeted mass spectrometry
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology