Targeted mass spectrometric analysis of N-terminally truncated isoforms generated via alternative translation initiation

FEBS Letters
Ryuji KobayashiJody Vykoukal

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.

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Citations

Sep 30, 2014·Proteomics·Daria GawronPetra Van Damme
Jul 9, 2011·The FEBS Journal·Petra Van DammeKris Gevaert
Feb 20, 2016·Molecular Systems Biology·Daria GawronPetra Van Damme
Feb 1, 2020·Trends in Biochemical Sciences·Annelies BogaertKris Gevaert

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