ArticleBiophysical journal2001
Distinct structural changes detected by X-ray fiber diffraction in stabilization of F-actin by lowering pH and increasing ionic strength.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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28 citing papers in PubMed, 44 citations in OpenAlex.
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- Mechanosensory entities and functionality of endothelial cells.Frontiers in cell and developmental biology · 2024Review
- Vascular mechanotransduction.Physiological reviews · 2023Review
- Effects of amiloride on acetylcholine-dependent arterial vasodilation evolve over time in mice on a high salt diet.Physiological reports · 2022Article
- Epithelial Sodium Channel and Salt-Sensitive Hypertension.Hypertension (Dallas, Tex. : 1979) · 2021Review
- Myopathy-Sensitive G-Actin Segment 227-235 Is Involved in Salt-Induced Stabilization of Contacts within the Actin Filament.International journal of molecular sciences · 2021Article
- It takes more than two to tango: mechanosignaling of the endothelial surface.Pflugers Archiv : European journal of physiology · 2020Review
- Salt-induced NaPflugers Archiv : European journal of physiology · 2017Article
- How to assign a (3 + 1)-dimensional superspace group to an incommensurately modulated biological macromolecular crystal.Journal of applied crystallography · 2017Article
- A pH- and ionic strength-dependent conformational change in the neck region regulates DNGR-1 function in dendritic cells.The EMBO journal · 2016Article
- X-Ray Fiber Diffraction Recordings from Oriented Demembranated Chlamydomonas Flagellar Axonemes.Biophysical journal · 2015Article
- Salt and gene expression: evidence for [Na+]i/[K+]i-mediated signaling pathways.Pflugers Archiv : European journal of physiology · 2015Review
- Salt controls endothelial and vascular phenotype.Pflugers Archiv : European journal of physiology · 2015Review
- Feedforward activation of endothelial ENaC by high sodium.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014Article
- The role of ENaC in vascular endothelium.Pflugers Archiv : European journal of physiology · 2014Review
- Aldosterone and vascular mineralocorticoid receptors: regulators of ion channels beyond the kidney.Hypertension (Dallas, Tex. : 1979) · 2014Review
- Blood pressure and amiloride-sensitive sodium channels in vascular and renal cells.Nature reviews. Nephrology · 2014Review
- Regulation of actin by ion-linked equilibria.Biophysical journal · 2013Review
- Electrostatics control actin filament nucleation and elongation kinetics.The Journal of biological chemistry · 2013Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lowering pH or raising salt concentration stabilizes the F-actin structure by increasing the free energy change associated with its polymerization. To understand the F-actin stabilization mechanism, we studied the effect of pH, salt concentration, and cation species on the F-actin structure. X-ray fiber diffraction patterns recorded from highly ordered F-actin sols at high density enabled us to detect minute changes of diffraction intensities and to precisely determine the helical parameters. F-actin in a solution containing 30 mM NaCl at pH 8 was taken as the control. F-actin at pH 8, 30 to 90 mM NaCl or 30 mM KCl showed a helical symmetry of 2.161 subunits per turn of the 1-start helix (12.968 subunits/6 turns). Lowering pH from 8 to 6 or replacing NaCl by LiCl altered the helical symmetry to 2.159 subunits per turn (12.952/6). The diffraction intensity associated with the 27-A meridional layer-line increased as the pH decreased but decreased as the NaCl concentration increased. None of the solvent conditions tested gave rise to significant changes in the pitch of the left-handed 1-start helix (approximately 59.8 A). The present results indicate that the two factors that stabilize F-actin, relatively low pH and high salt concentration, have distinct effects on the F-actin structure. Possible mechanisms will be discussed to understand how F-actin is stabilized under these conditions.
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