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2009 ; 48
(19
): 4009-18
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Porosome: the secretory portal in cells
#MMPMID19364126
Jena BP
Biochemistry
2009[May]; 48
(19
): 4009-18
PMID19364126
show ga
Porosomes are supramolecular, cup-shaped lipoprotein structures at the cell
plasma membrane, where membrane-bound secretory vesicles dock and fuse to release
intravesicular contents to the outside during cell secretion. The porosome
opening to the outside ranges from 150 nm in diameter in acinar cells of the
exocrine pancreas to 12 nm in neurons. In the past decade, the composition of the
porosome, its structure and dynamics at nanometer resolution in real time, and
its functional reconstitution into an artificial lipid membrane have been
described. Discovery of the universal secretory machinery in cells, the porosome,
came as no surprise since porosome-like "canaliculi" structures for secretion
from human platelets, the secretory machinery in single-cell organisms like the
secretion apparatus in bacteria and Toxoplasma gondii, and the contractile
vacuole in paramecium have been demonstrated. In this review, the discovery of
the porosome complex and the molecular mechanism of its function and how this
information provides a new understanding of cell secretion are discussed.
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