Key result
A covalently cross-linked profilin-actin heterodimer inhibited the intrinsic ATPase activity of actin and interfered with the elongation of actin filaments in a concentration-dependent manner.
The study supports a polymerization mechanism where the profilin-actin heterodimer binds to the (+)-end of actin filaments, followed by profilin dissociation and ATP hydrolysis.
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Informs models of actin filament assembly; leaves open relevance to cellular dynamics in vivo.
Nyman et al. (2002) studied this question. Cross-linked profilin-actin heterodimer vs. Unmodified profilin-actin and unmodified actin was evaluated on Actin filament elongation and ATPase activity. A covalently cross-linked profilin-actin heterodimer inhibited the intrinsic ATPase activity of actin and interfered with the elongation of actin filaments in a concentration-dependent manner.
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