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Table 2 Summary of literature of filamin-A in cancer metastasis

From: Complex roles of filamin-A mediated cytoskeleton network in cancer progression

Research system



Literatures reported the role of filamin-A in facilitating metastasis and cell locomotion

Meckel-Gruber syndrome patient

Filamin-A interacts with the cytoplasmic domain of meckelin, a transmembrane receptor, which is essential for neuronal migration and Wnt signalling


Hepatocellular carcinoma (HCC)

Comparative proteomics revealed that high level of filamin-A expression is associated with increased metastatic potentials of HCC cells.


Cancer tissues

By using a newly developed antibody that recognizes secreted variant of filamin-A, gradually increased levels of filamin-A was detected in normal breast tissue, localized and invasive breast cancer, which is associated with cancer progression.


Prostate cancer cell and tissue microarray

Filamin-A proteolysis results in nuclear localization of 90 kDa fragment, which is associated with decreased cancer metastasis, while elevated cytoplasmic levels of filamin-A was associated with enhanced metastatic potential


FlnA-knockdown rats

Filamin-A deficiency results in the abnormal migration, and then further causes disorganization of radial glia, which is the leading cause of PH pathogenesis.


NIH3T3 and HT1080 cells

Interaction of filamin-A with androgen receptor is essential for integrin β1 and FAK activation and cell migration induced by androgen stimulation


M2 and A7 melanoma cells

Filamin-A functions to stabilize cortical actin in vivo and is required for efficient cell locomotion


FlnA null mouse platelets

The interaction between FlnA and Syk regulates ITAM- and ITAM-like-containing receptor signaling which is essential for platelet spreading


M2 melanoma cells

R-Ras regulates migration through an interaction with filamin A in melanoma cells


EK-293 cells

Filamin A interacts with vimentin to regulation of cell adhesion to collagen through recycling beta1 integrins to cell membrane

[52, 53]

Melanoma and breast cancer cells and breast cancer TMA

Filamin-A deficiency in melanoma and breast cancer cells reduces not only cell motility and invasiveness, but also spontaneous and systemic metastasis in nude mouse xenograft. Decreased filamin-A expression levels in cancer cells are associated with better survival of distant metastasis-free in breast cancer patients.


Literatures reported the role of filamin-A inhibiting metastasis

Human fibrosarcoma cells

Filamin-A deficiency increases matrix metalloproteinase (MMP) activity and induces MMP2 activation, enhancing the ability of cells to remodel the ECM and increasing their invasive potential


HT1080 and Jurkat cells

Filamins play a role in cell migration and spreading through the interactions between filamins and transmembrane or signaling proteins, which is mediated at least in part by repeat 19 to 21.


A7 melanoma cells

Migfilin acts as a molecular switch to disconnect filamin from integrin for regulating integrin activation and dynamics of extracellular matrix-actin linkage.


Hematopoietic cell

ASB2 may regulate hematopoietic cell differentiation by modulating cell spreading and actin remodeling through targeting of filamins for degradation

[48, 118, 119]

Chinese hamster ovary cells

Tight filamin binding restricts integrin-dependent cell migration by inhibiting transient membrane protrusion and cell polarization.


A7 and M2 cells

Co-expression of CEACAM1-L and filamin A lead to a reduced RalA activation, focal adhesion turnover and cell migration


Primary melanoma cell line

Wnt5A activates calpain-1, leading to the cleavage of filamin A, which results in a remodeling of the cytoskeleton and an increase in melanoma cell motility.


ErbB2 overexpressed breast cancer cells and Breast TMA

Filamin-A deficiency in ErbB2-breast cancer cells reduces FAK turnover and cell motility. Down-regulation of filamin-A in stromal and base membrane is associated with breast cancer progression and invasive lymph node status