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FEBS Lett. 2009 Jul 21;583(14):2441-5. doi: 10.1016/j.febslet.2009.05.042. Epub 2009 May 28.

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

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1
FTN Institute, 1147 Mariner Cove, Sugar Land, TX 77498, USA. rkobayash@gmail.com

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.

PMID:
19481542
DOI:
10.1016/j.febslet.2009.05.042
[Indexed for MEDLINE]
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