title: Cofilin-induced unidirectional cooperative conformational changes in actin filaments revealed by high-speed atomic force microscopy.
abstract: High-speed atomic force microscopy was employed to observe structural changes in actin filaments induced by cofilin binding. Consistent with previous electron and fluorescence microscopic studies, cofilin formed clusters along actin filaments, where the filaments were 2-nm thicker and the helical pitch was ~25% shorter, compared to control filaments. Interestingly, the shortened helical pitch was propagated to the neighboring bare zone on the pointed-end side of the cluster, while the pitch on the barbed-end side was similar to the control. Thus, cofilin clusters induce distinctively asymmetric conformational changes in filaments. Consistent with the idea that cofilin favors actin structures with a shorter helical pitch, cofilin clusters grew unidirectionally toward the pointed-end of the filament. Severing was often observed near the boundaries between bare zones and clusters, but not necessarily at the boundaries.
authors: Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology, Tsukuba, Japan.
authors: Kien Xuan
authors: KX
authors: Ngo
authors: Department of Physics and Bio-AFM Frontier Research Center, Kanazawa University, Kanazawa, Japan.
authors: Noriyuki
authors: N
authors: Kodera
authors: Department of Biology, Graduate School of Science, Osaka City University, Osaka, Japan.
authors: Eisaku
authors: E
authors: Katayama
authors: Department of Physics and Bio-AFM Frontier Research Center, Kanazawa University, Kanazawa, Japan.
authors: Toshio
authors: T
authors: Ando
authors: Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology, Tsukuba, Japan.
authors: Taro Q P
authors: TQ
authors: Uyeda
mesh_terms: D008841:Actin Cytoskeleton / Q000737:chemistry* / Q000378:metabolism*; D051339:Actin Depolymerizing Factors / Q000378:metabolism*; D000818:Animals; D004023:Dictyostelium; D006801:Humans; D008051:Lipid Bilayers / Q000378:metabolism; D018625:Microscopy, Atomic Force / Q000379:methods*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D011817:Rabbits; D011993:Recombinant Fusion Proteins / Q000378:metabolism
chemical_list: D051339:Actin Depolymerizing Factors; D008051:Lipid Bilayers; D011993:Recombinant Fusion Proteins
keywords: S. cerevisiae; actin; biochemistry; biophysics; cofilin; cooperative conformational change; dictyostelium; human; myosin; structural biology
references: J Biol Chem. 1999 May 28;274(22):15538-46
references: 10336448
references: Annu Rev Biophys Biomol Struct. 2000;29:545-76
references: 10940259
references: Proc Natl Acad Sci U S A. 1975 Sep;72(9):3412-5
references: 1103145
references: Trends Biochem Sci. 2000 Dec;25(12):607-11
references: 11116187
references: J Cell Biol. 2001 Apr 2;153(1):75-86
references: 11285275
references: J Cell Biol. 2002 Mar 18;156(6):1065-76
references: 11901171
references: J Mol Biol. 2002 Nov 1;323(4):739-50
references: 12419261
references: J Neurosci. 2003 Apr 1;23(7):2527-37
references: 12684437
references: J Mol Biol. 1963 Sep;7:281-308
references: 14064165
references: Biophys Chem. 2004 Jul 1;110(1-2):119-28
references: 15223149
references: J Mol Biol. 2005 Feb 18;346(2):557-64
references: 15670604
references: J Mol Biol. 2005 Nov 11;353(5):990-1000
references: 16213521
references: J Mol Biol. 2006 Feb 17;356(2):325-34
references: 16375920
references: J Biol Chem. 2006 Apr 21;281(16):10727-36
references: 16490788
references: Cell Motil Cytoskeleton. 2006 Sep;63(9):533-42
references: 16847879
references: Mol Cell. 2006 Oct 6;24(1):13-23
references: 17018289
references: Curr Biol. 2007 May 15;17(10):825-33
references: 17493813
references: Physiol Rev. 2008 Jan;88(1):1-35
references: 18195081
references: Nat Nanotechnol. 2008 May;3(5):261-9
references: 18654521
references: J Mol Biol. 2009 Feb 13;386(1):149-62
references: 19100745
references: J Mol Biol. 2010 Feb 26;396(3):501-9
references: 19962990
references: Trends Cell Biol. 2010 Apr;20(4):187-95
references: 20133134
references: Nat Nanotechnol. 2010 Mar;5(3):208-12
references: 20154686
references: Biophys J. 2010 May 19;98(9):1893-901
references: 20441753
references: Methods Enzymol. 2010;475:541-64
references: 20627170
references: Biophys Rev. 2009 May 15;1(2):51-59
references: 20700473
references: J Biol Chem. 2010 Nov 19;285(47):36577-85
references: 20826799
references: Adv Biophys. 1990;26:51-73
references: 2082729
references: Nature. 2010 Nov 4;468(7320):72-6
references: 20935627
references: Cell. 2010 Oct 15;143(2):275-87
references: 20946985
references: Science. 2011 Jan 7;331(6013):80-3
references: 21148346
references: Nano Lett. 2011 Feb 9;11(2):825-7
references: 21175132
references: Curr Biol. 2011 May 24;21(10):862-8
references: 21530260
references: Curr Biol. 2011 Jul 26;21(14):R560-9
references: 21783039
references: Science. 2011 Aug 5;333(6043):755-8
references: 21817054
references: Eur J Cell Biol. 2011 Oct;90(10):797-804
references: 21820202
references: PLoS One. 2011;6(10):e26200
references: 22022566
references: Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20568-72
references: 22158895
references: Curr Biol. 2012 Feb 7;22(3):R96-101
references: 22321312
references: Nat Protoc. 2012 May 24;7(6):1193-206
references: 22635111
references: Histochem Cell Biol. 2012 Nov;138(5):725-36
references: 22790341
references: Biophys J. 2012 Jul 18;103(2):275-83
references: 22853905
references: Biophys J. 1990 Nov;58(5):1251-8
references: 2291944
references: J Biol Chem. 2013 Jan 18;288(3):1739-49
references: 23212920
references: Annu Rev Biophys. 2013;42:393-414
references: 23541159
references: Nat Rev Mol Cell Biol. 2013 Jul;14(7):405-15
references: 23778968
references: Eur J Cell Biol. 2013 Oct-Nov;92(10-11):333-8
references: 24252518
references: J Biochem. 1989 Nov;106(5):751-70
references: 2482289
references: Proc Natl Acad Sci U S A. 2014 Jul 8;111(27):9810-5
references: 24958883
references: Biophysics (Nagoya-shi). 2012 May 31;8:95-102
references: 27493525
references: J Biol Chem. 1988 Jan 15;263(2):817-25
references: 3335528
references: J Biol Chem. 1985 Nov 25;260(27):14410-2
references: 4055781
references: Proc R Soc Lond B Biol Sci. 1973 Feb 27;183(1070):39-58
references: 4144555
references: J Biol Chem. 1971 Aug 10;246(15):4866-71
references: 4254541
references: J Mol Biol. 1971 Nov 28;62(1):251-65
references: 4945533
references: Biochim Biophys Acta. 1969 Feb 25;172(2):311-8
references: 5775700
references: Biochemistry. 1982 Jul 20;21(15):3661-5
references: 6214272
references: Methods Enzymol. 1982;85 Pt B:55-71
references: 6214692
references: Cell Motil. 1982;2(1):1-8
references: 6890875
references: Nature. 1982 Jul 8;298(5870):131-5
references: 7201078
references: Science. 1993 Dec 24;262(5142):2027-30
references: 8266097
references: Biochemistry. 1993 Sep 28;32(38):9985-93
references: 8399167
references: Biochemistry. 1993 Sep 28;32(38):9994-10004
references: 8399168
references: Biochemistry. 1996 Sep 17;35(37):12038-45
references: 8810908
references: EMBO J. 1996 Nov 15;15(22):6069-74
references: 8947029
references: J Cell Biol. 1997 Mar 24;136(6):1307-22
references: 9087445
references: J Cell Biol. 1997 Aug 25;138(4):771-81
references: 9265645
references: J Biol Chem. 1998 Aug 14;273(33):20894-902
references: 9694836