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How depolymerization can promote polymerization: the case of actin and profilin
Author(s) -
Yarmola Elena G.,
Bubb Michael R.
Publication year - 2009
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.200900049
Subject(s) - profilin , actin , actin remodeling , polymerization , depolymerization , actin binding protein , mdia1 , microbiology and biotechnology , actin remodeling of neurons , cytoskeleton , chemistry , biophysics , extracellular , microfilament , biology , actin cytoskeleton , biochemistry , cell , polymer , polymer chemistry , organic chemistry
Rapid polymerization and depolymerization of actin filaments in response to extracellular stimuli is required for normal cell motility and development. Profilin is one of the most important actin‐binding proteins; it regulates actin polymerization and interacts with many cytoskeletal proteins that link actin to extracellular membrane. The molecular mechanism of profilin has been extensively considered and debated in the literature for over two decades. Here we discuss several accepted hypotheses regarding the mechanism of profilin function as well as new recently emerged possibilities. Thermal noise is routine in molecular world and unsurprisingly, nature has found a way to utilize it. An increasing amount of theoretical and experimental research suggests that fluctuation‐based processes play important roles in many cell events. Here we show how a fluctuation‐based process of exchange diffusion is involved in the regulation of actin polymerization.