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  PI(4,5)P2 dependent oligomerization of fibroblast growth factor 2 (FGF2) triggers the formation of a lipidic membrane pore implicated in unconventional secretion

Steringer, J. P., Bleicken, S., Andreas, H., Zacherl, S., Laussmann, M., Temmerman, K., et al. (2012). PI(4,5)P2 dependent oligomerization of fibroblast growth factor 2 (FGF2) triggers the formation of a lipidic membrane pore implicated in unconventional secretion. Journal of Biological Chemistry, 287(33), 27659-27669. doi:10.1074/jbc.M112.381939.

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Genre: Journal Article
Alternative Title : J. Biol. Chem.

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 Creators:
Steringer, J. P.1, Author
Bleicken, S.2, Author           
Andreas, H.1, Author
Zacherl, S.1, Author
Laussmann, M.1, Author
Temmerman, K.1, Author
Contreras, F. X.1, Author
Bharat, T. A.1, Author
Lechner, J.1, Author
Muller, H. M.1, Author
Briggs, J. A.1, Author
García-Sáez, A. J.2, Author           
Nickel, W.1, Author
Affiliations:
1Heidelberg University Biochemistry Center, Germany, ou_persistent22              
2Max Planck Research Group Membrane Biophysics, Max Planck Institute for Intelligent Systems, Max Planck Society, ou_1497659              

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Free keywords: MPI für Intelligente Systeme; Nachwuchsgruppe Garcia Sáez;
 Abstract: Fibroblast growth factor 2 (FGF2) is a critical mitogen with a central role in specific steps of tumor-induced angiogenesis. It is known to be secreted by unconventional means bypassing the ER/Golgi dependent secretory pathway. However,the mechanism of FGF2 membrane translocation into the extracellular space has remained elusive. Here we show that PI(4,5)P2 dependent membrane recruitment causes FGF2 to oligomerize which, in turn, triggers the formation of a lipidic membrane pore with a putative toroidal structure. This process is strongly upregulated by tyrosine phosphorylation of FGF2. Our findings explain key requirements of FGF2 secretion from living cells and suggest a novel self-sustained mechanism of protein translocation across membranes with a lipidic membrane pore being a transient translocation intermediate.

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Language(s): eng - English
 Dates: 2012
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 625306
DOI: 10.1074/jbc.M112.381939
 Degree: -

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Title: Journal of Biological Chemistry
  Alternative Title : J. Biol. Chem.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 287 (33) Sequence Number: - Start / End Page: 27659 - 27669 Identifier: -