Author(s): Martoglio B, Dobberstein B
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Abstract Export signal sequences target newly synthesized proteins to the endoplasmic reticulum of eukaryotic cells and the plasma membrane of bacteria. All signal sequences contain a hydrophobic core region, but, despite this, they show great variation in both overall length and amino acid sequence. Recently, it has become clear that this variation allows signal sequences to specify different modes of targeting and membrane insertion and even to perform functions after being cleaved from the parent protein. This review argues that signal sequences are not simply greasy peptides but sophisticated, multipurpose peptides containing a wealth of functional information.
This article was published in Trends Cell Biol
and referenced in Journal of Proteomics & Bioinformatics