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  ATP-dependent membrane assembly of F-actin facilitates membrane fusion

Jahraus, A., Egeberg, M., Hinner, B., Habermann, A., Sackman, E., Pralle, A., et al. (2001). ATP-dependent membrane assembly of F-actin facilitates membrane fusion. Molecular Biology of the Cell, 12(1), 155-170. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/11160830.

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Genre: Journal Article
Alternative Title : ATP-dependent membrane assembly of F-actin facilitates membrane fusion

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MolBiolCell_12_2001_155.pdf (Any fulltext), 832KB
 
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 Creators:
Jahraus, Andrea, Author
Egeberg, Morten, Author
Hinner, Bernhard, Author
Habermann, Anja, Author
Sackman, Erich, Author
Pralle, Arnd, Author
Faulstich, Heinz1, Author              
Rybin, Vladimir, Author
Defacque, Hélène, Author
Griffiths, Gareth, Author
Affiliations:
1Department of Molecular Cell Research, Max Planck Institute for Medical Research, Max Planck Society, ou_1497703              

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 Abstract: We recently established an in vitro assay that monitors the fusion between latex-bead phagosomes and endocytic organelles in the presence of J774 macrophage cytosol (Jahraus et al., 1998). Here, we show that different reagents affecting the actin cytoskeleton can either inhibit or stimulate this fusion process. Because the membranes of purified phagosomes can assemble F-actin de novo from pure actin with ATP (Defacque et al., 2000a), we focused here on the ability of membranes to nucleate actin in the presence of J774 cytosolic extracts. For this, we used F-actin sedimentation, pyrene actin assays, and torsional rheometry, a biophysical approach that could provide kinetic information on actin polymerization and gel formation. We make two major conclusions. First, under our standard in vitro conditions (4 mg/ml cytosol and 1 mM ATP), the presence of membranes actively catalyzed the assembly of cytosolic F-actin, which assembled into highly viscoelastic gels. A model is discussed that links these results to how the actin may facilitate fusion. Second, cytosolic actin paradoxically polymerized more under ATP depletion than under high-ATP conditions, even in the absence of membranes; we discuss these data in the context of the well described, large increases in F-actin seen in many cells during ischemia.

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Language(s): eng - English
 Dates: 2000-10-122000-05-222000-11-082001-01-12
 Publication Status: Published in print
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 Rev. Type: Peer
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Title: Molecular Biology of the Cell
  Other : Mol. Biol. Cell
Source Genre: Journal
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Publ. Info: American Society for Cell Biology
Pages: - Volume / Issue: 12 (1) Sequence Number: - Start / End Page: 155 - 170 Identifier: ISSN: 1059-1524
CoNE: https://pure.mpg.de/cone/journals/resource/954927716372_1