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J. Biol. Chem., Vol. 260, Issue 27, 14410-14412, 11, 1985
N Yonezawa, E Nishida and H Sakai
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.
pH control of actin polymerization by cofilin
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