Abstract
Soluble hydrolases represent the main proteins of lysosomes and vacuoles and are essential to sustain the lytic properties of these organelles typical for the eukaryotic organisms. The sorting of these proteins from ER residents and secreted proteins is controlled by highly specific receptors to avoid mislocalization and subsequent cellular damage. After binding their soluble cargo in the early stage of the secretory pathway, receptors rely on their own sorting signals to reach their target organelles for ligand delivery, and to recycle back for a new round of cargo recognition. Although signals in cargo and receptor molecules have been studied in human, yeast and plant model systems, common denominators and specific examples of diversification have not been systematically explored. This review aims to fill this niche by comparing the structure and the function of lysosomal/vacuolar sorting receptors (VSRs) from these three organisms.
Highlights
The plant vacuole was first discovered in 1676 by a Dutch scientist Antonie van Leeuwenhoek
It was generally accepted that plant cells have at least two types of vacuoles: a storage vacuole (SV) and a lytic vacuole (LV) [8] this is being challenged by new findings which favour the one unique vacuole type per cell
Lysosomes and vacuoles are morphologically different, they do share a number of crucial functions in human, yeast and plants cells
Summary
The plant vacuole was first discovered in 1676 by a Dutch scientist Antonie van Leeuwenhoek. Because vacuoles appear as optically empty sacs filling the volume of the cell they have been named from the Latin ‘vacuus’ meaning empty It was only 300 years later that Christian de Duve, a Belgian biochemist, discovered mammalian lysosomes entirely based on biochemical methods [2] and as he calls it himself by ‘a gift of serendipity’ while working on insulin [3]. Soluble proteins are diverted from the secretory bulk-flow of proteins due to the presence of sorting signals that are recognized by specific membrane spanning receptors to initiate transport to the degradative organelles These signals are surface structures either directly displayed by the folded polypeptide (often in fungi and plants) or indirectly via post-translational modification of sugar chains (in vertebrates). Not all vacuolar proteins in yeast contain such a motif, indicating that alternative signals may exist in yeast [27,28]
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