Počet záznamů: 1
Key steps in unconventional secretion of fibroblast growth factor 2 reconstituted with purified components
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SYSNO ASEP 0478166 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Key steps in unconventional secretion of fibroblast growth factor 2 reconstituted with purified components Tvůrce(i) Steringer, J. P. (DE)
Lange, S. (DE)
Čujová, Sabína (UFCH-W) ORCID
Šachl, Radek (UFCH-W) RID, ORCID
Poojari, C. (FI)
Lolicato, F. (FI)
Beutel, O. (DE)
Müller, H.-M. (DE)
Unger, S. (DE)
Coskun, U. (DE)
Honigmann, A. (DE)
Vattulainen, I. (FI)
Hof, Martin (UFCH-W) RID, ORCID
Freund, Ch. (DE)
Nickel, W. (DE)Číslo článku e28985 Zdroj.dok. eLife. - : eLife - ISSN 2050-084X
Roč. 6, č. 2017 (2017)Poč.str. 36 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova Unconventional protein secretion ; Fibroblast Growth Factor 2 ; Protein translocation across membranes Vědní obor RIV CF - Fyzikální chemie a teoretická chemie Obor OECD Physical chemistry CEP GC14-03141J GA ČR - Grantová agentura ČR Způsob publikování Open access Institucionální podpora UFCH-W - RVO:61388955 UT WOS 000410744600001 EID SCOPUS 85029789831 DOI 10.7554/eLife.28985.001 Anotace 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. Pracoviště Ústav fyzikální chemie J.Heyrovského Kontakt Michaela Knapová, michaela.knapova@jh-inst.cas.cz, Tel.: 266 053 196 Rok sběru 2018
Počet záznamů: 1