There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.
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.