4.5 Review Book Chapter

Unconventional Mechanisms of Protein Transport to the Cell Surface of Eukaryotic Cells

Journal

ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY
Volume 24, Issue -, Pages 287-308

Publisher

ANNUAL REVIEWS
DOI: 10.1146/annurev.cellbio.24.110707.175320

Keywords

unconventional protein secretion; nonclassical export; protein targeting; local protein biosythesis; Golgi-independent trafficking; fibroblast growth factor-1 and-2; galectin; thioredoxin; HMGB-1; annexin; Ist2

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The classical secretion of soluble proteins and transport of integral membrane proteins to the cell surface require transit into and though the endoplasmic reticulum and the Golgi apparatus. Signal peptides or transmembrane domains target proteins for translocation into the lumen or insertion into the membrane of the endoplasmic reticulum, respectively. Here we discuss two mechanisms of unconventional protein targeting to plasma membranes, i.e., transport processes that are active in the absence of a functional Golgi system. We first focus on integral membrane proteins that are inserted into the endoplasmic reticulum but that, however are transported to plasma membranes in a Golgi-independent manner. We then discuss soluble secretory proteins that are secreted from cells without any involvement of the endoplasmic reticulum and the Golgi apparatus.

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