TY  - JOUR
AU  - Galkin, V.E.
AU  - Orlova, A.
AU  - Kudryashov, D.S.
AU  - Solodukhin, A.
AU  - Reisler, E.
AU  - Schröder, G.F.
AU  - Egelman, E.H.
TI  - Remodeling of actin filaments by ADF/cofilin proteins
JO  - Proceedings of the National Academy of Sciences of the United States of America
VL  - 108
SN  - 0027-8424
CY  - Washington, DC
PB  - Academy
M1  - PreJuSER-19044
SP  - 20568 - 20572
PY  - 2011
N1  - This work was supported by National Institutes of Health Grants GM081303 (E. H. E.) and GM077190 (E.R.).
AB  - Cofilin/ADF proteins play key roles in the dynamics of actin, one of the most abundant and highly conserved eukaryotic proteins. We used cryoelectron microscopy to generate a 9-Å resolution three-dimensional reconstruction of cofilin-decorated actin filaments, the highest resolution achieved for a complex of F-actin with an actin-binding protein. We show that the cofilin-induced change in the filament twist is due to a unique conformation of the actin molecule unrelated to any previously observed state. The changes between the actin protomer in naked F-actin and in the actin-cofilin filament are greater than the conformational changes between G- and F-actin. Our results show the structural plasticity of actin, suggest that other actin-binding proteins may also induce large but different conformational changes, and show that F-actin cannot be described by a single molecular model.
KW  - Actin Depolymerizing Factors: chemistry
KW  - Actins: chemistry
KW  - Cofilin 2: chemistry
KW  - Cryoelectron Microscopy: methods
KW  - Cytoskeleton: chemistry
KW  - Gene Library
KW  - Humans
KW  - Microscopy, Electron: methods
KW  - Models, Molecular
KW  - Molecular Conformation
KW  - Muscle, Skeletal: metabolism
KW  - Polymers: chemistry
KW  - Protein Conformation
KW  - Protein Structure, Secondary
KW  - Actin Depolymerizing Factors (NLM Chemicals)
KW  - Actins (NLM Chemicals)
KW  - Cofilin 2 (NLM Chemicals)
KW  - Polymers (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:22158895
C2  - pmc:PMC3251117
UR  - <Go to ISI:>//WOS:000298289400064
DO  - DOI:10.1073/pnas.1110109108
UR  - https://juser.fz-juelich.de/record/19044
ER  -