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Cofilin, a 21,000 molecular weight actin-regulatory protein (Nishida, E., Maekawa, S., and Sakai, H. (1984) Biochemistry 23, 5307-5313), was here shown to be capable of reversibly controlling actin polymerization and depolymerization in a pH-sensitive manner. When cofilin was reacted with F-actin at different pH, the depolymerized actin concentration (= monomeric actin concentration) was higher at elevated pH. At pH less than 7.3, the monomeric actin concentrations did not exceed approximately 1 microM even in the presence of excess amounts of cofilin, whereas at pH greater than 7.3 it increased in proportion to the concentration of cofilin added, and complete depolymerization of F-actin occurred by the addition of an excess amount of cofilin. Moreover, in the presence of cofilin, rapid interconversion of monomeric and polymeric forms of actin can be induced by simply changing the pH of the medium. Thus, this study provides a new possible mechanism regulating actin polymerization, pH control.
N Yonezawa, and
E Nishida, and
H Sakai
September 2006,
Cell motility and the cytoskeleton,
N Yonezawa, and
E Nishida, and
H Sakai
August 2010,
F1000 biology reports,
N Yonezawa, and
E Nishida, and
H Sakai
April 2004,
Science (New York, N.Y.),
N Yonezawa, and
E Nishida, and
H Sakai
February 2007,
Journal of molecular biology,
N Yonezawa, and
E Nishida, and
H Sakai
September 1998,
Biochemistry,
N Yonezawa, and
E Nishida, and
H Sakai
April 2010,
Proceedings of the National Academy of Sciences of the United States of America,
N Yonezawa, and
E Nishida, and
H Sakai
July 2003,
Experimental cell research,
N Yonezawa, and
E Nishida, and
H Sakai
December 2008,
The Journal of biological chemistry,
N Yonezawa, and
E Nishida, and
H Sakai
January 2021,
Biochemical and biophysical research communications,
N Yonezawa, and
E Nishida, and
H Sakai
February 2000,
The Journal of cell biology,
