Die molekulare Entschlüsselung unkonventioneller Sekretionsmechanismen

The vast majority of secretory proteins is characterized by N-terminal signal peptides that allow for co-translational translocation into the lumen of the endoplasmic reticulum, the initial compartment of the classical ER/Golgi-dependent secretory pathway. However, extracellular proteins with fundam...

Full description

Saved in:
Bibliographic Details
Main Authors: Steringer, Julia P. (Author) , Müller, Hans-Michael (Author) , Nickel, Walter (Author)
Format: Article (Journal)
Language:German
Published: 19 June 2014
In: Biospektrum
Year: 2014, Volume: 20, Issue: 4, Pages: 400-403
ISSN:1868-6249
DOI:10.1007/s12268-014-0456-8
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1007/s12268-014-0456-8
Get full text
Author Notes:Julia P. Steringer, Hans-Michael Müller & Walter Nickel
Description
Summary:The vast majority of secretory proteins is characterized by N-terminal signal peptides that allow for co-translational translocation into the lumen of the endoplasmic reticulum, the initial compartment of the classical ER/Golgi-dependent secretory pathway. However, extracellular proteins with fundamental physiological functions in immune surveillance and tissue organization have been identified that lack signal peptides. The molecular mechanisms by which these unconventional secretory proteins reach the extracellular space are beginning to emerge.
Item Description:Gesehen am 11.12.2020
Physical Description:Online Resource
ISSN:1868-6249
DOI:10.1007/s12268-014-0456-8