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The startling properties of fibroblast growth factor 2: how to exit mammalian cells without a signal peptide at hand

For a long time, protein transport into the extracellular space was believed to strictly depend on signal peptide-mediated translocation into the lumen of the endoplasmic reticulum. More recently, this view has been challenged, and the molecular mechanisms of unconventional secretory processes are b...

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Bibliographic Details
Main Authors: La Venuta, Giuseppe (Author) , Zeitler, Marcel (Author) , Steringer, Julia P. (Author) , Müller, Hans-Michael (Author) , Nickel, Walter (Author)
Format: Article (Journal)
Language:English
Published: September 28, 2015
In: The journal of biological chemistry
Year: 2015, Volume: 290, Issue: 45, Pages: 27015-27020
ISSN:1083-351X
DOI:10.1074/jbc.R115.689257
Online Access:Resolving-System, lizenzpflichtig, Volltext: https://doi.org/10.1074/jbc.R115.689257
Verlag, lizenzpflichtig, Volltext: http://www.jbc.org/content/290/45/27015
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Author Notes:Giuseppe La Venuta, Marcel Zeitler, Julia P. Steringer, Hans-Michael Müller, and Walter Nickel
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Summary:For a long time, protein transport into the extracellular space was believed to strictly depend on signal peptide-mediated translocation into the lumen of the endoplasmic reticulum. More recently, this view has been challenged, and the molecular mechanisms of unconventional secretory processes are beginning to emerge. Here, we focus on unconventional secretion of fibroblast growth factor 2 (FGF2), a secretory mechanism that is based upon direct protein translocation across plasma membranes. Through a combination of genome-wide RNAi screening approaches and biochemical reconstitution experiments, the basic machinery of FGF2 secretion was identified and validated.
Item Description:Gesehen am 05.06.2020
Physical Description:Online Resource
ISSN:1083-351X
DOI:10.1074/jbc.R115.689257

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