Adenomatous polyposis coli protein nucleates actin assembly and synergizes with the formin mDia1

被引:133
作者
Okada, Kyoko [1 ]
Bartolini, Francesca [5 ]
Deaconescu, Alexandra M. [2 ,3 ]
Moseley, James B. [1 ]
Dogic, Zvonimir [4 ]
Grigorieff, Nikolaus [2 ,3 ]
Gundersen, Gregg G. [5 ]
Goode, Bruce L. [1 ]
机构
[1] Brandeis Univ, Rosenstiel Basic Med Sci Res Ctr, Dept Biol, Waltham, MA 02454 USA
[2] Brandeis Univ, Rosenstiel Basic Med Sci Res Ctr, Howard Hughes Med Inst, Waltham, MA 02454 USA
[3] Brandeis Univ, Rosenstiel Basic Med Sci Res Ctr, Dept Biochem, Waltham, MA 02454 USA
[4] Brandeis Univ, Rosenstiel Basic Med Sci Res Ctr, Dept Phys, Waltham, MA 02454 USA
[5] Columbia Univ, Dept Pathol & Cell Biol, New York, NY 10032 USA
基金
美国国家卫生研究院;
关键词
TUMOR-SUPPRESSOR; APC PROTEIN; IN-VIVO; CELL; PROFILIN; FILAMENTS; MICROTUBULES; MIGRATION; SPIRE; ASSOCIATION;
D O I
10.1083/jcb.201001016
中图分类号
Q2 [细胞生物学];
学科分类号
071013 [干细胞生物学];
摘要
T he tumor suppressor protein adenomatous polyposis coli (APC) regulates cell protrusion and cell migration, processes that require the coordinated regulation of actin and microtubule dynamics. APC localizes in vivo to microtubule plus ends and actin-rich cortical protrusions, and has well-documented direct effects on microtubule dynamics. However, its potential effects on actin dynamics have remained elusive. Here, we show that the C-terminal "basic" domain of APC (APC-B) potently nucleates the formation of actin filaments in vitro and stimulates actin assembly in cells. Nucleation is achieved by a mechanism involving APC-B dimerization and recruitment of multiple actin monomers. Further, APC-B nucleation activity is synergistic with its in vivo binding partner, the formin mDia1. Together, APC-B and mDia1 overcome a dual cellular barrier to actin assembly imposed by profilin and capping protein. These observations define a new function for APC and support an emerging view of collaboration between distinct actin assembly-promoting factors with complementary activities.
引用
收藏
页码:1087 / 1096
页数:10
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