Key steps in unconventional secretion of fibroblast growth factor 2 reconstituted with purified components

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F17%3A00478166" target="_blank" >RIV/61388955:_____/17:00478166 - isvavai.cz</a>

Result on the web

<a href="http://dx.doi.org/10.7554/eLife.28985.001" target="_blank" >http://dx.doi.org/10.7554/eLife.28985.001</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.7554/eLife.28985.001" target="_blank" >10.7554/eLife.28985.001</a>

Result language

angličtina

Original language name

Key steps in unconventional secretion of fibroblast growth factor 2 reconstituted with purified components

Original language description

FGF2 is secreted from cells by an unconventional secretory pathway. This process is mediated by direct translocation across the plasma membrane. Here, we define the minimal molecular machinery required for FGF2 membrane translocation in a fully reconstituted inside-out vesicle system. FGF2 membrane translocation is thermodynamically driven by PI(4,5)P2-induced membrane insertion of FGF2 oligomers. The latter serve as dynamic translocation intermediates of FGF2 with a subunit number in the range of 8-12 FGF2 molecules. Vectorial translocation of FGF2 across the membrane is governed by sequential and mutually exclusive interactions with PI(4,5)P2 and heparan sulfates on opposing sides of the membrane. Based on atomistic molecular dynamics simulations, we propose a mechanism that drives PI(4,5)P2 dependent oligomerization of FGF2. Our combined findings establish a novel type of self-sustained protein translocation across membranes revealing the molecular basis of the unconventional secretory pathway of FGF2.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10403 - Physical chemistry

Project

<a href="/en/project/GC14-03141J" target="_blank" >GC14-03141J: Exploring the structure function relationship of membrane-pore-forming FGF2 oligomers - a single molecule approach</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2017

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

eLife

ISSN

2050-084X

e-ISSN

—

Volume of the periodical

6

Issue of the periodical within the volume

2017

Country of publishing house

GB - UNITED KINGDOM

Number of pages

36

Pages from-to

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UT code for WoS article

000410744600001

EID of the result in the Scopus database

2-s2.0-85029789831