HOW PROFILIN PROMOTES ACTIN FILAMENT ASSEMBLY IN THE PRESENCE OF THYMOSIN-BETA-4

被引：475
作者：
PANTALONI, D
CARLIER, MF
机构：
[1] Laboratoire d'Enzymologie, Centre National de la Recherche Scientifique
来源：
CELL | 1993年 / 75卷 / 05期
关键词：
D O I：
10.1016/0092-8674(93)90544-Z
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The role of profilin in the regulation of actin assembly has been reexamined. The affinity of profilin for ATP-actin appears 10-fold higher than previously thought. in the presence of ATP, the participation of the profilin-actin complex to filament elongation at the barbed end is linked to a decrease in the steady-state concentration of globular actin. This surprising effect is made possible by the involvement of the irreversible ATP hydrolysis accompanying actin polymerization. As a consequence, in the presence of thymosin beta4 (Tbeta4), low amounts of profilin promote extensive actin assembly off of the pool of actin-Tbeta4 complex. When barbed ends are capped, profilin simply sequesters globular actin. A model is proposed for the function of profilin in actin-based motility.
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页码：1007 / 1014
页数：8
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