Abstract：
:Porosomes are the universal secretory portals at the cell plasma membrane, where membrane-bound secretory vesicles transiently dock and fuse to expel intravesicular contents to the outside during cell secretion. In the past decade, the neuronal porosome complex, a 10-15nm cup-shaped lipoprotein structure has been isolated, its partial composition and 3D contour map determined, and it has been functionally reconstituted into artificial lipid membrane. Here we further determine the composition of the neuronal porosome proteome using immunoisolation and gel filtration chromatography, followed by tandem mass spectrometry. Results from the study demonstrate nearly 40 proteins to constitute the neuronal porosome proteome. Furthermore, interaction of proteins within the porosome and their resulting arrangement is predicted. The association and dissociation of proteins at the porosome following stimulation of cell secretion demonstrate the dynamic nature of the organelle.
journal_name
J Proteomicsjournal_title
Journal of proteomicsauthors
Lee JS,Jeremic A,Shin L,Cho WJ,Chen X,Jena BPdoi
10.1016/j.jprot.2012.05.017subject
Has Abstractpub_date
2012-07-16 00:00:00pages
3952-62issue
13eissn
1874-3919issn
1876-7737pii
S1874-3919(12)00329-6journal_volume
75pub_type
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journal_title：Journal of proteomics
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journal_title：Journal of proteomics
pub_type： 杂志文章,评审
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journal_title：Journal of proteomics
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journal_title：Journal of proteomics
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pub_type： 杂志文章
doi：10.1016/j.jprot.2011.05.025
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journal_title：Journal of proteomics
pub_type： 杂志文章,评审
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journal_title：Journal of proteomics
pub_type： 杂志文章
doi：10.1016/j.jprot.2009.06.014
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journal_title：Journal of proteomics
pub_type： 杂志文章
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journal_title：Journal of proteomics
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doi：10.1016/j.jprot.2019.103401
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journal_title：Journal of proteomics
pub_type： 杂志文章
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journal_title：Journal of proteomics
pub_type： 杂志文章
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更新日期：2017-08-23 00:00:00
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journal_title：Journal of proteomics
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