|
|
|
||||
| Home Help Feedback Subscriptions Archive Search Table of Contents | |||||
In this issue |
|
Actin treadmilling the continuous removal of actin monomers from the pointed ends of filaments and their reincorporation at barbed ends is essential for cell motility. The process is accelerated by the actin-binding protein ADF/cofilin, which stimulates the release of actin monomers from pointed ends. Kenji Moriyama and Ichiro Yahara have investigated the role of another factor that could play a role in treadmilling CAP1 an adenylyl-cyclase-binding protein whose C-terminus has been shown to inhibit actin polymerization (see p. 1591). They show that CAP1 is part of a complex that contains ADF/cofilin, actin-interacting protein 1 (Aip1) and actin. In addition, they show that the CAP1 N-terminus can stimulate removal of actin from the pointed ends of filaments whereas the C-terminus promotes filament assembly at barbed ends. Another important finding is that the CAP1 N- and C-termini cooperate to relieve cofilin-mediated inhibition of ADP-ATP exchange on G-actin. This is likely to increase the availability of easily polymerizable monomers and indicates that during treadmilling CAP1 has important roles in both actin depolymerization and recycling.
Related articles in JCS:
| ||||||||||||||||||||||||||||||||||||||||||||