Skip to main content
Log in

Die molekulare Entschlüsselung unkonventioneller Sekretionsmechanismen

  • Wissenschaft · Special: Zellbiologie
  • Proteinsekretion
  • Published:
BIOspektrum Aims and scope

Abstract

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.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Literatur

  1. Muesch A, Hartmann E, Rohde K et al. (1990) A novel pathway for secretory proteins? Trends Biochem Sci 15:86–88

    Article  CAS  PubMed  Google Scholar 

  2. Zhang M, Schekman R (2013) Cell biology. Unconventional secretion, unconventional solutions. Science 340:559–561

    CAS  Google Scholar 

  3. Engling A, Backhaus R, Stegmayer C et al. (2002) Biosynthetic FGF-2 is targeted to non-lipid raft microdomains following translocation to the extracellular surface of CHO cells. J Cell Sci 115:3619–3631

    Article  CAS  PubMed  Google Scholar 

  4. Nickel W (2005) Unconventional secretory routes: direct protein export across the plasma membrane of mammalian cells. Traffic 6:607–614

    Article  CAS  PubMed  Google Scholar 

  5. Schäfer T, Zentgraf H, Zehe C et al. (2004) Unconventional secretion of fibroblast growth factor 2 is mediated by direct translocation across the plasma membrane of mammalian cells. J Biol Chem 279:6244–6251

    Article  PubMed  Google Scholar 

  6. Backhaus R, Zehe C, Wegehingel S et al. (2004) Unconventional protein secretion: membrane translocation of FGF-2 does not require protein unfolding. J Cell Sci 117:1727–1736

    Article  CAS  PubMed  Google Scholar 

  7. Nickel W, Seedorf M (2008) Unconventional mechanisms of protein transport to the cell surface of eukaryotic cells. Annu Rev Cell Dev Biol 24:287–308

    Article  CAS  PubMed  Google Scholar 

  8. Temmerman K, Ebert AD, Muller HM et al. (2008) A direct role for phosphatidylinositol-4,5-bisphosphate in unconventional secretion of fibroblast growth factor 2. Traffic 9:1204–1217

    Article  CAS  PubMed  Google Scholar 

  9. Nickel W (2007) Unconventional secretion: an extracellular trap for export of fibroblast growth factor 2. J Cell Sci 120:2295–2299

    Article  CAS  PubMed  Google Scholar 

  10. Zehe C, Engling A, Wegehingel S et al. (2006) Cellsurface heparan sulfate proteoglycans are essential components of the unconventional export machinery of FGF-2. Proc Natl Acad Sci USA 103:15479–15484

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  11. Ebert AD, Laussmann M, Wegehingel S et al. (2010) Tec-kinase-mediated phosphorylation of fibroblast growth factor 2 is essential for unconventional secretion. Traffic 11:813–826

    Article  CAS  PubMed  Google Scholar 

  12. Nickel W, Rabouille C (2009) Mechanisms of regulated unconventional protein secretion. Nat Rev Mol Cell Biol 10:148–155

    Article  CAS  PubMed  Google Scholar 

  13. Nickel W (2011) The unconventional secretory machinery of fibroblast growth factor 2. Traffic 12:799–805

    Article  CAS  PubMed  Google Scholar 

  14. Steringer JP, Bleicken S, Andreas H et al. (2012) Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2)-dependent oligomerization of fibroblast growth factor 2 (FGF2) triggers the formation of a lipidic membrane pore implicated in unconventional secretion. J Biol Chem 287:27659–27669

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  15. Rabouille C, Malhotra V, Nickel W (2012) Diversity in unconventional protein secretion. J Cell Sci 125:5251–5255

    Article  CAS  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Walter Nickel.

Additional information

Julia P. Steringer Jahrgang 1983. Biologiestudium an der Universität Heidelberg und an der ETH Zürich, Schweiz. 2012 Promotion, danach Postdoc am Biochemie-Zentrum der Universität Heidelberg.

Hans-Michael Müller Jahrgang 1959. Biologiestudium an der Universität Heidelberg. 1989 Promotion. 1990 Postdoc am Zentrum für Molekulare Biologie Heidelberg (ZMBH). 1991–1995 Postdoc am Institut für Parasitologie der Universität La Sapientia, Rom, Italien. 1996–2005 wissenschaftlicher Mitarbeiter am European Molecular Biology Laboratory (EMBL), Heidelberg. 2001 Habilitation an der Universität Heidelberg. 2006 wissenschaftlicher Mitarbeiter am ZMBH. Seit 2007 Senior Scientist in der Arbeitsgruppe Nickel am Biochemie-Zentrum der Universität Heidelberg (BZH).

Walter Nickel Jahrgang 1964. Biologiestudium an der Universität Göttingen. 1994 Promotion. 1994–1997 Postdoc am Institut für Biochemie I, Universität Heidelberg. 1997–2000 Postdoc am Memorial Sloan Kettering Cancer Center New York, USA. 2001 Habilitation im Fach Biochemie an der Universität Heidelberg. Seit 2004 Professor für Biochemie, Biochemie-Zentrum der Universität Heidelberg (BZH).

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Steringer, J.P., Müller, HM. & Nickel, W. Die molekulare Entschlüsselung unkonventioneller Sekretionsmechanismen. Biospektrum 20, 400–403 (2014). https://doi.org/10.1007/s12268-014-0456-8

Download citation

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12268-014-0456-8

Navigation