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  Electrostatics Control Actin Filament Nucleation and Elongation Kinetics

Crevenna, A., Naredi-Rainer, N., Schoenichen, A., Dzubiella, J., Barber, D. L., Lamb, D. C., et al. (2013). Electrostatics Control Actin Filament Nucleation and Elongation Kinetics. JOURNAL OF BIOLOGICAL CHEMISTRY, 288(17), 12102-12113. doi:10.1074/jbc.M113.456327.

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 Creators:
Crevenna, Alvaro1, Author              
Naredi-Rainer, Nikolaus2, Author
Schoenichen, Andre2, Author
Dzubiella, Joachim2, Author
Barber, Diane L.2, Author
Lamb, Don C.2, Author
Wedlich-Söldner, Roland1, Author              
Affiliations:
1Wedlich-Söldner, Roland / Cellular Dynamics and Cell Patterning, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565174              
2external, ou_persistent22              

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Free keywords: FLUORESCENCE CORRELATION SPECTROSCOPY; PHOTON-COUNTING HISTOGRAM; NA-H EXCHANGE; NA+/H+ EXCHANGER; CELL-MIGRATION; POINTED END; BARBED END; ACIDIC PH; F-ACTIN; POLYMERIZATION
 Abstract: The actin cytoskeleton is a central mediator of cellular morphogenesis, and rapid actin reorganization drives essential processes such as cell migration and cell division. Whereas several actin-binding proteins are known to be regulated by changes in intracellular pH, detailed information regarding the effect of pH on the actin dynamics itself is still lacking. Here, we combine bulk assays, total internal reflection fluorescence microscopy, fluorescence fluctuation spectroscopy techniques, and theory to comprehensively characterize the effect of pH on actin polymerization. We show that both nucleation and elongation are strongly enhanced at acidic pH, with a maximum close to the pI of actin. Monomer association rates are similarly affected by pH at both ends, although dissociation rates are differentially affected. This indicates that electrostatics control the diffusional encounter but not the dissociation rate, which is critical for the establishment of actin filament asymmetry. A generic model of protein-protein interaction, including electrostatics, explains the observed pH sensitivity as a consequence of charge repulsion. The observed pH effect on actin in vitro agrees with measurements of Listeria propulsion in pH-controlled cells. pH regulation should therefore be considered as a modulator of actin dynamics in a cellular environment.

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Language(s): eng - English
 Dates: 2013
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000318157600043
DOI: 10.1074/jbc.M113.456327
 Degree: -

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Title: JOURNAL OF BIOLOGICAL CHEMISTRY
Source Genre: Journal
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Publ. Info: 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA : AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Pages: - Volume / Issue: 288 (17) Sequence Number: - Start / End Page: 12102 - 12113 Identifier: ISSN: 0021-9258