The Uncoupling of the Effects of Formins on the Local and Global Dynamics of Actin Filaments
Open accessAbstract
In this study, experiments were carried out in the conventional and saturation-transfer electron paramagnetic resonance (EPR) time domains to explore the effect of mDia1-FH2 formin fragments on the dynamic and conformational properties of actin filaments. Conventional EPR measurements showed that addition of formin to actin filaments produced local conformational changes in the vicinity of Cys-374 by increasing the flexibility of the protein matrix in the environment of the label. The results indicated that it was the binding of formin to the barbed end that resulted in these conformational changes. The conventional EPR results obtained with actin labeled on the Lys-61 site showed that the binding of formins could only slightly affect the structure of the subdomain 2 of actin, reflecting the heterogeneity of the formin-induced conformational changes. Saturation transfer EPR measurements revealed that the binding of formins decreased the torsional flexibility of the actin filaments in the microsecond time range. We concluded that changes in the local and the global conformational fluctuations of the actin filaments are associated with the binding of formins to actin. The results on the two EPR time domains showed that the effects of formins on the substantially different types of motions were uncoupled.
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Actin contains five cysteine residues, and C374 incorporates more than 70% of spin labels during spin labeling reactions.
“Although actin contains five cysteine residues, a number of studies has shown that the C-terminal C374, which is in close proximity to actin’s hydrophobic pocket (Fig. 2d), is most solvent exposed (Supplementary Fig. 4a, b) and incorporates more than 70% of spin labels during spin labeling reactions37–41.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [38]
The section “Rotational motions in actin observed by spin labels” states that Cys-374 incorporated more than 70% of maleimide spin labels under the conditions used in the paper. Our copy does not state that actin has five cysteine residues, and the reported percentage is specific to those labeling conditions rather than spin labeling generally. (LLM, conf=0.86)
Experimental — accuracy not yet measuredCys374 of actin is solvent exposed and can be labeled with the spin label MTSSL.
“Cys374 of actin is solvent exposed and can be labeled with the spin label MTSSL37–41.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [38]
The Introduction and “Rotational motions in actin observed by spin labels” report that a spin label attaches to Cys-374 and that this site incorporated more than 70% of the labels under the experimental conditions. This supports its accessibility for labeling, but the paper uses maleimide spin label (MSL), not MTSSL, and does not explicitly describe Cys-374 as solvent exposed. Page numbers were not available in our copy. (LLM, conf=0.88)
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Research works printed but not linked: 1
- [3]3. Sheterline, P., J. Clayton, and S.J.C. 1998. Protein profiles. Actin. P. Sheterline, J. Clayton, and J.C. Sparrow, editors. New York: Oxford Univ. Press.
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Cabrales Fontela, Y., Kadavath, H., Biernat, J., Riedel, D., Mandelkow, E., & Zweckstetter, M. (2017) · Nature Communications · doi:10.1038/s41467-017-02230-8 · Cited by 148 · see citing works
- Authors
- Kupi, T., Gróf, P., Nyitrai, M., & Belágyi, J.
- Affiliations
- University of Pecs (HU)
- Semmelweis University (HU)
- Corresponding author
- Belágyi, József
- Venue
- Biophysical Journal
- Publisher
- Elsevier BV
- Published
- 2009-04
- Volume
- 96
- Issue
- 7
- Pages
- 2901-2911
- ISSN
- 0006-3495 (ISSN-L)
- PMC
- PMC2711290
- OpenAlex
- W2088943592
- Cited by
- 19
- References
- 0
- Citations by year
- 2024: 1 · 2023: 1 · 2018: 2 · 2017: 1 · 2016: 1 · 2015: 1 · 2013: 3 · 2012: 3
- FWCI
- 1.33
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biophysical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Hungarian Scientific Research Fund (K60186, K60968)
- Hungarian Science Foundation
- Wellcome Trust
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Electron Spin Resonance Studies
- Keywords
- formins, F-actin, torsional flexibility, saturation transfer EPR, actin filament dynamics
- MeSH terms
- Formins, Actins, Animals, Carrier Proteins, Electron Spin Resonance Spectroscopy, Actin Cytoskeleton, Motion, Movement, Rotation, Spin Labels, Temperature, Time Factors, Mice
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