Mechanism of interaction of Acanthamoeba actophorin (ADF/Cofilin) with actin filaments. Export

@article{Blanchoin_1999, abstract = {We characterized the interaction of Acanthamoeba actophorin, a member of ADF/cofilin family, with filaments of amoeba and rabbit skeletal muscle actin. The affinity is about 10 times higher for muscle actin filaments (Kd = 0.5 microM) than amoeba actin filaments (Kd = 5 microM) even though the affinity for muscle and amoeba Mg-ADP-actin monomers (Kd = 0.1 microM) is the same (Blanchoin, L., and Pollard, T. D. (1998) J. Biol. Chem. 273, 25106-25111). Actophorin binds slowly (k+ = 0.03 microM-1 s-1) to and dissociates from amoeba actin filaments in a simple bimolecular reaction, but binding to muscle actin filaments is cooperative. Actophorin severs filaments in a concentration-dependent fashion. Phosphate or BeF3 bound to ADP-actin filaments inhibit actophorin binding. Actophorin increases the rate of phosphate release from actin filaments more than 10-fold. The time course of the interaction of actophorin with filaments measured by quenching of the fluorescence of pyrenyl-actin or fluorescence anisotropy of rhodamine-actophorin is complicated, because severing, depolymerization, and repolymerization follows binding. The 50-fold higher affinity of actophorin for Mg-ADP-actin monomers (Kd = 0.1 microM) than ADP-actin filaments provides the thermodynamic basis for driving disassembly of filaments that have hydrolyzed ATP and dissociated gamma-phosphate.}, address = {Structural Biology Laboratory, The Salk Institute for Biological Studies, La Jolla, California 92037, USA.}, author = {Blanchoin, L. and Pollard, T. D.}, citeulike-article-id = {681314}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/10336448}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=10336448}, day = {28}, issn = {0021-9258}, journal = {J Biol Chem}, keywords = {actin, adf}, month = {May}, number = {22}, pages = {15538--15546}, posted-at = {2006-06-02 11:37:23}, priority = {2}, title = {Mechanism of interaction of Acanthamoeba actophorin (ADF/Cofilin) with actin filaments.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/10336448}, volume = {274}, year = {1999} }

TY - JOUR ID - Blanchoin_1999 L3 - citeulike-article-id:681314 N2 - We characterized the interaction of Acanthamoeba actophorin, a member of ADF/cofilin family, with filaments of amoeba and rabbit skeletal muscle actin. The affinity is about 10 times higher for muscle actin filaments (Kd = 0.5 microM) than amoeba actin filaments (Kd = 5 microM) even though the affinity for muscle and amoeba Mg-ADP-actin monomers (Kd = 0.1 microM) is the same (Blanchoin, L., and Pollard, T. D. (1998) J. Biol. Chem. 273, 25106-25111). Actophorin binds slowly (k+ = 0.03 microM-1 s-1) to and dissociates from amoeba actin filaments in a simple bimolecular reaction, but binding to muscle actin filaments is cooperative. Actophorin severs filaments in a concentration-dependent fashion. Phosphate or BeF3 bound to ADP-actin filaments inhibit actophorin binding. Actophorin increases the rate of phosphate release from actin filaments more than 10-fold. The time course of the interaction of actophorin with filaments measured by quenching of the fluorescence of pyrenyl-actin or fluorescence anisotropy of rhodamine-actophorin is complicated, because severing, depolymerization, and repolymerization follows binding. The 50-fold higher affinity of actophorin for Mg-ADP-actin monomers (Kd = 0.1 microM) than ADP-actin filaments provides the thermodynamic basis for driving disassembly of filaments that have hydrolyzed ATP and dissociated gamma-phosphate. IS - 22 JF - J Biol Chem SN - 0021-9258 AD - Structural Biology Laboratory, The Salk Institute for Biological Studies, La Jolla, California 92037, USA. EP - 15546 TI - Mechanism of interaction of Acanthamoeba actophorin (ADF/Cofilin) with actin filaments. VL - 274 SP - 15538 KW - actin KW - adf AU - Blanchoin, L AU - Pollard, TD PY - 1999/05/28/ UR - http://view.ncbi.nlm.nih.gov/pubmed/10336448 ER -