Literature DB >> 17786931

Secretion without Golgi.

Igor Prudovsky1, Francesca Tarantini, Matteo Landriscina, David Neivandt, Raffaella Soldi, Aleksandr Kirov, Deena Small, Karuppanan Muthusamy Kathir, Dakshinamurthy Rajalingam, Thallapuranam Krishnaswamy Suresh Kumar.   

Abstract

A growing number of proteins devoid of signal peptides have been demonstrated to be released through the non-classical pathways independent of endoplasmic reticulum and Golgi. Among them are two potent proangiogenic cytokines FGF1 and IL1alpha. Stress-induced transmembrane translocation of these proteins requires the assembly of copper-dependent multiprotein release complexes. It involves the interaction of exported proteins with the acidic phospholipids of the inner leaflet of the cell membrane and membrane destabilization. Not only stress, but also thrombin treatment and inhibition of Notch signaling stimulate the export of FGF1. Non-classical release of FGF1 and IL1alpha presents a promising target for treatment of cardiovascular, oncologic, and inflammatory disorders. 2007 Wiley-Liss, Inc.

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Year:  2008        PMID: 17786931      PMCID: PMC2613191          DOI: 10.1002/jcb.21513

Source DB:  PubMed          Journal:  J Cell Biochem        ISSN: 0730-2312            Impact factor:   4.429


  167 in total

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4.  Molecular mechanism of inhibition of nonclassical FGF-1 export.

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  55 in total

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9.  Protein folding does not prevent the nonclassical export of FGF1 and S100A13.

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10.  NMR characterization of copper and lipid interactions of the C2B domain of synaptotagmin I-relevance to the non-classical secretion of the human acidic fibroblast growth factor (hFGF-1).

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