Cofilin binding to muscle and non-muscle actin filaments: isoform-dependent cooperative interactions - PubMed (original) (raw)
. 2005 Feb 18;346(2):557-64.
doi: 10.1016/j.jmb.2004.11.065. Epub 2004 Dec 30.
Affiliations
- PMID: 15670604
- DOI: 10.1016/j.jmb.2004.11.065
Cofilin binding to muscle and non-muscle actin filaments: isoform-dependent cooperative interactions
Enrique M De La Cruz. J Mol Biol. 2005.
Abstract
I have monitored equilibrium binding of human cofilin to rabbit skeletal muscle (alpha) and human non-muscle (85% beta, 15% gamma) actin filaments from the quenching of pyrene actin fluorescence. Filament binding is cooperative and stoichiometric (i.e. one cofilin molecule per actin subunit) for both actin isoforms. The Hill coefficient for binding to betagamma-actin filaments (n(H)=3.5) is greater than for muscle actin (n(H)=2.3). Analysis of equilibrium binding using a nearest-neighbor cooperativity model indicates that the intrinsic affinities for binding to an isolated site are comparable (10-14 microM) for both filament isoforms but the cooperative free energy is greater for binding betagamma-actin filaments. The predicted cofilin cluster sizes and filament binding densities are small at concentrations of cofilin where efficient filament severing is observed, indicating that a few bound cofilin molecules are sufficient to destabilize the filament lattice and promote fragmentation. The analysis used in this study provides a framework for evaluating proton and ion linkage and effects of regulatory proteins on cofilin binding and severing of actin filaments.
Similar articles
- Energetics and kinetics of cooperative cofilin-actin filament interactions.
Cao W, Goodarzi JP, De La Cruz EM. Cao W, et al. J Mol Biol. 2006 Aug 11;361(2):257-67. doi: 10.1016/j.jmb.2006.06.019. Epub 2006 Jun 27. J Mol Biol. 2006. PMID: 16843490 - Determining the differences in actin binding by human ADF and cofilin.
Yeoh S, Pope B, Mannherz HG, Weeds A. Yeoh S, et al. J Mol Biol. 2002 Jan 25;315(4):911-25. doi: 10.1006/jmbi.2001.5280. J Mol Biol. 2002. PMID: 11812157 - ADF/cofilin weakens lateral contacts in the actin filament.
McGough A, Chiu W. McGough A, et al. J Mol Biol. 1999 Aug 20;291(3):513-9. doi: 10.1006/jmbi.1999.2968. J Mol Biol. 1999. PMID: 10448032 Review.
Cited by
- Origin of twist-bend coupling in actin filaments.
De La Cruz EM, Roland J, McCullough BR, Blanchoin L, Martiel JL. De La Cruz EM, et al. Biophys J. 2010 Sep 22;99(6):1852-60. doi: 10.1016/j.bpj.2010.07.009. Biophys J. 2010. PMID: 20858430 Free PMC article. - Cofilin Signaling in the CNS Physiology and Neurodegeneration.
Namme JN, Bepari AK, Takebayashi H. Namme JN, et al. Int J Mol Sci. 2021 Oct 3;22(19):10727. doi: 10.3390/ijms221910727. Int J Mol Sci. 2021. PMID: 34639067 Free PMC article. Review. - Torsional stress generated by ADF/cofilin on cross-linked actin filaments boosts their severing.
Wioland H, Jegou A, Romet-Lemonne G. Wioland H, et al. Proc Natl Acad Sci U S A. 2019 Feb 12;116(7):2595-2602. doi: 10.1073/pnas.1812053116. Epub 2019 Jan 28. Proc Natl Acad Sci U S A. 2019. PMID: 30692249 Free PMC article. - Cofilin-linked changes in actin filament flexibility promote severing.
McCullough BR, Grintsevich EE, Chen CK, Kang H, Hutchison AL, Henn A, Cao W, Suarez C, Martiel JL, Blanchoin L, Reisler E, De La Cruz EM. McCullough BR, et al. Biophys J. 2011 Jul 6;101(1):151-9. doi: 10.1016/j.bpj.2011.05.049. Biophys J. 2011. PMID: 21723825 Free PMC article. - The remodelling of actin composition as a hallmark of cancer.
Suresh R, Diaz RJ. Suresh R, et al. Transl Oncol. 2021 Jun;14(6):101051. doi: 10.1016/j.tranon.2021.101051. Epub 2021 Mar 21. Transl Oncol. 2021. PMID: 33761369 Free PMC article. Review.