Porosome: the universal molecular machinery for cell secretion.
Porosomes are supramolecular, lipoprotein structures at the cell plasma membrane, where membrane-bound secretory vesicles transiently dock and fuse to release inravesicular contents to the outside during cell secretion. The mouth of the porosome opening to the outside, range in size from 150 nm in diameter in acinar cells of the exocrine pancreas, to 12 nm in neurons, which dilates during cell secretion, returning to its resting size following completion of the process. In the past decade, the composition of the porosome, its structure and dynamics at nm resolution and in real time, and its functional reconstitution into artificial lipid membrane, have all been elucidated. In this mini review, the discovery of the porosome, its structure, function, isolation, chemistry, and reconstitution into lipid membrane, the molecular mechanism of secretory vesicle swelling and fusion at the base of porosomes, and how this new information provides a paradigm shift in our understanding of cell secretion, is discussed.
Jena
Bhanu P
BP
Department of Physiology, Wayne State University School of Medicine, Detroit, MI 48201, USA. bjena@med.wayne.edu
D000818:Animals; D002462:Cell Membrane / Q000502:physiology*; D002477:Cells / Q000378:metabolism*; D006801:Humans; D008051:Lipid Bilayers / Q000378:metabolism; D052066:N-Ethylmaleimide-Sensitive Proteins / Q000502:physiology; D015388:Organelles / Q000502:physiology; D046790:Pancreas, Exocrine / Q000378:metabolism; D050600:SNARE Proteins / Q000378:metabolism / Q000648:ultrastructure; D022142:Secretory Vesicles / Q000502:physiology / Q000648:ultrastructure; D013574:Synaptosomes / Q000502:physiology / Q000648:ultrastructure
D008051:Lipid Bilayers; D050600:SNARE Proteins; D052066:N-Ethylmaleimide-Sensitive Proteins