期刊
CURRENT BIOLOGY
卷 20, 期 4, 页码 339-345出版社
CELL PRESS
DOI: 10.1016/j.cub.2009.12.035
关键词
-
资金
- core Cancer Research UK
- Medical Research Council UK [G117/569]
- Association for International Cancer Research [07-0438]
- Medical Research Council [G117/569] Funding Source: researchfish
- MRC [G117/569] Funding Source: UKRI
Fascin is an actin-bundling protein involved in filopodia assembly and cancer invasion and metastasis of multiple epithelial cancer types. Fascin forms stable actin bundles with slow dissociation kinetics in vitro [1] and is regulated by phosphorylation of serine 39 by protein kinase C (PKC) [2]. Cancer cells use invasive finger-like protrusions termed invadopodia to invade into and degrade extracellular matrix. Invadopodia have highly dynamic actin that is assembled by both Arp2/3 complex and formins [3, 4]; they also contain components of membrane trafficking machinery such as dynamin and cortactin [5] and have been compared with focal adhesions and podosomes [6, 7]. We show that fascin is an integral component of invadopodia and that it is important for the stability of actin in invadopodia. The phosphorylation state of fascin at S39, a PKC site, contributes to its regulation at invadopodia. We further implicate fascin in invasive migration into collagen I-Matrigel gels and particularly in cell types that use an elongated mesenchymal type of motility in 3D. We provide a potential molecular mechanism for how fascin increases the invasiveness of cancer cells, and we compare invadopodia with invasive filopod-like structures in 3D.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据