期刊
JOURNAL OF CELL SCIENCE
卷 128, 期 24, 页码 4601-4614出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.175760
关键词
Fascin; Cytoskeleton; Actin; Microtubule; Focal adhesion; Migration; Focal adhesion kinase
类别
资金
- Royal Society
- Breast Cancer Campaign [2009NovPhD31]
- Medical Research Council [MR/J000647/1]
- Biotechnology and Biological Sciences Research Council [BB/F020635/2] Funding Source: researchfish
- Cancer Research UK [15703] Funding Source: researchfish
- Medical Research Council [MR/J000647/1] Funding Source: researchfish
- BBSRC [BB/F020635/2] Funding Source: UKRI
- MRC [MR/J000647/1] Funding Source: UKRI
Fascin is an actin-binding and bundling protein that is highly upregulated in most epithelial cancers. Fascin promotes cell migration and adhesion dynamics in vitro and tumour cell metastasis in vivo. However, potential non-actin bundling roles for fascin remain unknown. Here, we showfor the first timethat fascin can directly interact with the microtubule cytoskeleton and that this does not depend upon fascin-actin bundling. Microtubule binding contributes to fascin-dependent control of focal adhesion dynamics and cell migration speed. We also show that fascin forms a complex with focal adhesion kinase (FAK, also known as PTK2) and Src, and that this signalling pathway lies downstream of fascin-microtubule association in the control of adhesion stability. These findings shed light on newnon act-independent roles for fascin and might have implications for the design of therapies to target fascin in metastatic disease.
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