Calponin repeats regulate actin filament stability and formation of podosomes in smooth muscle cells

被引：149

作者：

Gimona, M ^{[1
]}

Kaverina, I ^{[1
]}

Resch, GP ^{[1
]}

Vignal, E ^{[1
]}

Burgstaller, G ^{[1
]}

机构：

[1] Austrian Acad Sci, Inst Mol Biol, Dept Cell Biol, A-5020 Salzburg, Austria

来源：

MOLECULAR BIOLOGY OF THE CELL | 2003年 / 14卷 / 06期

关键词：

D O I：

10.1091/mbc.E02-11-0743

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 [细胞生物学]; 090102 [作物遗传育种];

摘要：

Phorbol ester induces, actin cytoskeleton rearrangements in cultured vascular smooth muscle cells. Calponin and SM22 alpha are major components of differentiated smooth muscle and potential regulators of actin cytoskeleton interactions. Here we show that actin fibers decorated with h1 CaP remain stable, whereas SM22 alpha-decorated actin bundles undergo rapid reorganization into podosomes within 30 min of PDBu exposure. Ectopic expression of GFP alpha-actinin had no effect on the stability of the actin cytoskeleton and alpha-actinin was transported rapidly into PDBu-induced, podosomes. Our results demonstrate the involvement of CaP and SM22 alpha in coordinating the balance between st;iilization and dynamics of the actin cytoskeleton in mammalian smooth muscle. We provide, evidence for the existence of two functionally distinct actin filament popua lations and introduce a molecular mechanism for the stabilization of the actin cytoskeleton by the unique actin-bindinginterface formed by calponin family-specific CLIK23 repeats.

引用

页码：2482 / 2491

页数：10

共 40 条

[1]

Coordination of protrusion and translocation of the keratocyte involves rolling of the cell body [J].