Roles of fascin in cell adhesion and motility
Dept of Cell Biology, NC1-110, Lerner Research Institute, Cleveland Clinic Foundation, 9500 Euclid Avenue, Cleveland, Ohio 44195, USA. Current Opinion in Cell Biology
(Impact Factor: 8.47).
11/2004; 16(5):590-6. DOI: 10.1016/j.ceb.2004.07.009
Many cell interactions depend on the assembly of cell protrusions; these include cell attachment and migration in the extracellular matrix, cell-cell communication, and the ability of cells to sense their local environment. Cell protrusions are extensions of the plasma membrane that are supported internally by actin-based structures that impart mechanical stiffness. Fascin is a small, globular actin-bundling protein that has emerging roles in diverse forms of cell protrusions and in cytoplasmic actin bundles. The fascin-actin interaction is under complex regulation from the extracellular matrix, peptide factors and other actin-binding proteins. Recent developments advance our understanding of the multifaceted regulation of fascin and the roles of fascin-containing structures in cell adhesion, motility and invasion in the life of vertebrate organisms.
Available from: Ling Yang
- "Key words: Bone marrow mesenchymal stem cells, Fascin, Migration capacity, Specific short hairpin RNA, Wuzhishan pig mechanisms to avoid allogeneic rejection (Ryan et al. 2005), and BMMSC transplantation has therapeutic benefits to many kinds of diseases such as Alzheimer's disease, heart infarction, and rheumatoid arthritis (Lee et al. 2010, Loffredo et al. 2011, Papadopoulou et al. 2012). Fascin, encoded by the FSCN1 gene in human, is an actin cross-linking protein that shares no homology with other actin-bundling proteins, which contributes to cell migration by providing rigidity to filopodia and microspikes (Adams 2004). Fascin is a structural protein which is found in mesenchyme, nervous, and retinal tissue, which plays a central role in the regulation of cell adhesion, migration and invasion through bundling to actin molecules (Jayo and Parsons 2010). "
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ABSTRACT: The bone marrow mesenchymal stem cells (BM-MSCs) from Wuzhishan pig (WZSP) with knockdown expression of Fascin were used to make out the role Fascin gene in migratory potential of BM-MSCs. The role of Fascin gene is well established in cellular migration, but it is unclear for its activity in porcine BM-MSCs. At present study, BM-MSCs were isolated from femur and tibia of the WZSP with about 42 day-old, and had been evaluated by previous study. At first, 4 vectors encoding different short hairpin RNA (shRNA) for Fascin were designed to knock down Fascin, and qRT-PCR was employed to detect the expression of Fascin mRNA by BM-MSCs after transfection, and the vector with best interference effect was selected to be used in the following experiments. And then, the effect of knock down Fascin was further determined through Western blot using Fascin antibody. Finally, the migration capacity of the BM-MSCs was evaluated through scratch assay and transwell migration assay. The results showed that the specific shRNA for knocking down Fascin efficiently was found for the BM-MSCs from WZSP, and Fascin was involved in regulating the migration capacity of the BM-MSCs in vitro , which may be useful for the BM-MSCs from WZSP to be utilized in regenerative therapy for human.
Available from: Ruohong Xia
- "These molecules are the downstream signaling proteins in the signaling pathways that regulate the invasive or structural actin cytoskeleton. Among these proteins, fascin, which binds to the filaments in filopodia, plays a key role in establishing these filaments, whose over-expression generally induces greater filopodial growth –. Arp2/3, which is usually found in lamellipodia, acts as a nucleation core for the assembly of new branch filaments, through which the complex stimulates filament polymerization in the cell leading edge , . "
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ABSTRACT: In this article, we have examined the motility-related effects of weak power frequency magnetic fields (MFs) on the epidermal growth factor receptor (EGFR)-sensitive motility mechanism, including the F-actin cytoskeleton, growth of invasive protrusions and the levels of signal molecules in human amniotic epithelial (FL) cells. Without extracellular EGF stimulation, the field stimulated a large growth of new protrusions, especially filopodia and lamellipodia, an increased population of vinculin-associated focal adhesions. And, an obvious reduction of stress fiber content in cell centers was found, corresponding to larger cell surface areas and decreased efficiency of actin assembly of FL cells in vitro, which was associated with a decrease in overall F-actin content and special distributions. These effects were also associated with changes in protein content or distribution patterns of the EGFR downstream motility-related signaling molecules. All of these effects are similar to those following epidermal growth factor (EGF) stimulation of the cells and are time dependent. These results suggest that power frequency MF exposure acutely affects the migration/motility-related actin cytoskeleton reorganization that is regulated by the EGFR-cytoskeleton signaling pathway. Therefore, upon the MF exposure, cells are likely altered to be ready to transfer into a state of migration in response to the stimuli.
Available from: Hinke A.B. Multhaupt
- "Fibronectin-mediated activation of PKCα inhibits the formation of nascent adhesions and cell protrusions by phosphorylating fascin (at Ser 39 ) to block its association with actin and thereby its functioning in F-actin polymerization (Adams 2004). A dynamic activity of PKCα is probably required in this context. "
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ABSTRACT: Cell adhesion to extracellular matrix is a complex process involving protrusive activity driven by the actin cytoskeleton, engagement of specific receptors, followed by signaling and cytoskeletal organization. Thereafter, contractile and endocytic/recycling activities may facilitate migration and adhesion turnover. Focal adhesions, or focal contacts, are widespread organelles at the cell-matrix interface. They arise as a result of receptor interactions with matrix ligands, together with clustering. Recent analysis shows that focal adhesions contain a very large number of protein components in their intracellular compartment. Among these are tyrosine kinases, which have received a great deal of attention, whereas the serine/threonine kinase protein kinase C has received much less. Here the status of protein kinase C in focal adhesions and cell migration is reviewed, together with discussion of its roles and potential substrates.
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