Isoform diversity in the Arp2/3 complex determines actin filament dynamics

被引:146
作者
Abella, Jasmine V. G. [1 ]
Galloni, Chiara [1 ]
Pernier, Julien [2 ]
Barry, David J. [1 ]
Kjaer, Svend [3 ]
Carlier, Marie-France [2 ]
Way, Michael [1 ]
机构
[1] Francis Crick Inst, Lincolns Inn Fields Lab, Cellular Signalling & Cytoskeletal Funct, London WC2A 3LY, England
[2] CNRS, I2BC, Lab Enzymol & Biochim Struct, F-91198 Gif Sur Yvette, France
[3] Francis Crick Inst, Lincolns Inn Fields Lab, Struct Biol Sci Technol Platform, London WC2A 3LY, England
基金
欧洲研究理事会; 加拿大健康研究院;
关键词
ALDRICH-SYNDROME PROTEIN; DEPOLYMERIZING FACTOR COFILIN; WASP FAMILY PROTEINS; N-WASP; VACCINIA VIRUS; CORONIN; 1B; WASP/SCAR PROTEINS; CORTACTIN; ACTIVATION; NUCLEATION;
D O I
10.1038/ncb3286
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The Arp2/3 complex consists of seven evolutionarily conserved subunits (Arp2, Arp3 and ARPC1-5) and plays an essential role in generating branched actin filament networks during many different cellular processes. In mammals, however, the ARPC1 and ARPC5 subunits are each encoded by two isoforms that are 67% identical. This raises the possibility that Arp2/3 complexes with different properties may exist. We found that Arp2/3 complexes containing ARPC1B and ARPC5L are significantly better at promoting actin assembly than those with ARPC1A and ARPC5, both in cells and in vitro. Branched actin networks induced by complexes containing ARPC1B or ARPC5L are also disassembled similar to 2-fold slower than those formed by their counterparts. This difference reflects the ability of cortactin to stabilize ARPC1B- and ARPC5L- but not ARPC1A- and ARPC5-containing complexes against coronin-mediated disassembly. Our observations demonstrate that the Arp2/3 complex in higher eukaryotes is actually a family of complexes with different properties.
引用
收藏
页码:76 / +
页数:13
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