Fascin Promotes Filopodia Formation Independent Of Its Role In Actin Bundling
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Filopodia and adhesion in cancer cell motility
Actin cytoskeleton, myosin-X and β1-integrins in filopodia formation. (1) β1-integrins are endocytosed from the plasma-membrane and recycled back to cell surface via tubulating actin-dependent
The Bundling Activity of Vasodilator-Stimulated
of actin filaments, thus favoring the formation of dense F-actin meshworks, whereas formins efficiently elongate linear actin fila-ments (1). Although formin function could be clearly correlated with the establishment of actin cables and stress fibers (2, 3), we only recently began to understand its role in filopodium formation (4-6).
Fascin promotes filopodia formation independent of its role
interaction with actin and altered filopodia dynamics within carcinoma cells. These data reveal an evolution-arily conserved role for this regulatory region and unveil a function for fascin, uncoupled from actin bundling, at the distal end of filopodia. Fascin promotes filopodia formation independent of its role in actin bundling
November 4-5 Allerton Park & Retreat Center Monticello, IL
Fascin, an actin binding protein, is a regulator of many developmental processes and contributes to cancer aggressiveness. Functioning to bundle actin filaments, Fascin promotes cell motility, invasion, and adhesion through its canonical role of forming filopodia and invadopodia. Fascin controls cell
Docosahexaenoic acid inhibits 12- O-tetradecanoylphorbol-13
fascin in actin filaments in filopodia and lamellipodia of the snail Helisoma are increased by TPA . Furthermore, modulation of PKC activity by TPA leads to altered fascin localization and the formation of fascin-mediated microspikes in LLC-PK1 kidney epithelial cells and C2C12 skeletal myoblasts . To date, however, whether
Improving fascin inhibitors to block tumor cell migration and
Fascin protein is the main actin-bundling protein in ﬁlopodia. Here we report the development of fascin-speciﬁc small-mol-ecules that inhibit the interaction between fascin and actin. These inhibitors block the in vitro actin-binding and actin-bundling activities of fascin, tumor cell migration and tu-mor metastasis in mouse models.
Fascin 1 is dispensable for developmental and tumour angiogenesis
Sep 16, 2013 We suggest that fascin 1 facilitates angiogenesis via its well-known effects on filopodia formation and migration, but that overall the role of fascin in angiogenesis is not greatly limiting for development or tumour formation. Results and Discussion Fascin 1-null C57BL/6 mice display partial neonatal death and
Cofilin cooperates with fascin to disassemble filopodial
formation. Cofilin efficiently severs actin filaments in fascin-crosslinked bundles A previous study showed that spontaneously formed actin bundles were more resistant to cofilin-mediated severing than single filaments in vitro (Michelot et al., 2007). However, the effects of filopodial bundling proteins such as fascin on cofilin-
Prostaglandins regulate nuclear localization of Fascin and
promotes Enabled processivity model was used to elucidate Fascin s bundling-independent role in promoting actin bundle formation and filopodia initiation (Zanet. et al., 2012), and in
Filopodia-independent roles of the actin bundling protein
Filopodia-independent roles of the actin bundling protein fascin in promoting cell motility Abstract Fascin is an actin bundling protein whose overexpression has in recent years been systematically linked to increased metastasis and poor outcome in cancer patients. It is well
SCIENTIFIC REPORT 2014
Fascin is regulated by slug, promotes progression of pancreatic cancer in mice, and is associated with patient outcomes. Gastroenterology 2014; 146: 1386-96 e1-17 This paper provides strong evidence that the actin-bundling protein fascin is regulated by the transcription factor slug and involved in pancreatic tumour formation and metastatic spread.
Stress-induced cleavage of Myc promotes cancer cell survival
induction of the actin-bundling protein fascin, formation of filopodia, and increased cell motility all mediators of tumor metastasis. Myc-nick-induced survival, autophagy, and motility require Myc box II (MBII), a region of Myc-nick that recruits acetyltransferases that in turn modify cytoplasmic proteins, including a-tubulin and ATG3.
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role of TGFb in normal tissue. Written by Isaac Bruce, Commissioning Editor. Source: Sun J, He H, Xiong Y et al. Fascin protein is critical for Transforming Growth Factor b protein-induced inva-sion and filopodia formation in spindle-shaped tumor cells. J. Biol. Chem. 286, 38865 38875 (2011). Fascin-ating study could lead to new cancer therapies
actin bundling protein that localizes to microspikes, filopodia and actin-based protrusions underneath the plasma mem-brane. Fascin has received a lot of atten-tion among cytoskeletal proteins because multiple clinical studies have implicated its expression in cancer progression and metastasis. This may be because fascin
RESEARCH ARTICLE Open Access Association of fascin-1 with
Background: Fascin-1 is an actin-bundling protein expressed in many human carcinomas, although absent from most normal epithelia. Fascin-1 promotes filopodia formation, migration and invasion in carcinoma cells; in mouse xenograft tumor models it contributes to metastasis. Fascin-1 is an interesting candidate biomarker for aggressive,
Viral exploitation of actin: force-generation and scaffolding
The actin cytoskeleton exists as a polarized array of filaments, termed F-actin, in dynamic equilibrium with a globular actin, or G-actin, pool. Polymerization of the F-actin ﬁ lament occurs predominately at the barbed end (also known as the plus end), while depolymerization occurs predominantly at the pointed end (also known as the minus end).
Swiprosin-1 stimulates cancer invasion and metastasis by
membrane dynamics as an actin binding and bundling protein indicates a potential role in invasion and metastasis, although its specific function in cancer cell progression
Fascin 1 is dispensable for developmental and tumour angiogenesis
filopodia formation during sprouting. We thus propose that fascin 1 expression promotes angiogenesis via filopodia formation, but is largely dispensable for both normal and tumour angiogenesis. 2013. Published by The Company of Biologists Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License
RESEARCH ARTICLE Open Access A novel Rho-dependent pathway
Fascin-1 is a prominent actin-bundling protein that char- acterizes the filopodia, microspikes, and dendrites of mesenchymal, neuronal, and dendritic cells, respectively, and also contributes to filopodia, podosomes, and invado- podia in migratory vascular smooth muscle cells and cancer cells [1-4].
F-actin bundles direct the initiation and orientation of
peripheral F-actin bundles/filopodia containing fascin-1 serve as templates for formation and orientation of lamel-lipodia. Accordingly, modulation of fascin-1 expression tunes cell shape, quantified as the number of morphologi-cal extensions. Ratiometric imaging reveals that F-actin bundles/filopodia play both structural and signaling roles,
Fascin1 expression in high-grade serous ovarian carcinoma is
actin-bundling protein and is an important regulatory element in the maintenance and stability of parallel bundles of filamentous actin in a variety of cellular contexts (3).
Promotes cross-linkage of parallel actin filaments during the formation of cell protrusions (lamellipodia and filopodia), and therefore plays an important role in regulating cell migration. It has been reported that fascin may also regulate filopodia formation by a mechanism independent of its actin-bundling functions, though less
Myosin-X Is a Molecular Motor That Functions in Filopodia
and can stimulate filopodia formation, presumably because of their anticapping activity (10, 11). Filopodia formation also involves actin bundling, and fascin appears to serve as a major actin bundling protein in filopodia (8). MyolO is a vertebrate-specific MyTH4-FERM myosin that is expressed in most tissues, exhibits a striking localization
A Cytoplasmyc Player in Colon Cancer - Fred Hutch
of fascin, an actin-bundling protein often upregulated in cancer. Consistent with these observations, Myc-nick-expressing cells displayed increased motility. Furthermore, analysis of Myc expression in human colorectal cancer revealed that Myc-nick is often localized to the invasive edges of tumors.
Encapsulation of the cytoskeleton: towards mimicking the
Actin filaments are bundled by crosslinkers such as fascin. The mechanics of the cell membrane and therefore cell shape however is governed by the cell cortex, shell-like networks of crosslinked and branched actin bound to the membrane. Dynamic actin-membrane binding proteins such as ezrin, profilin, and cofilin 56, 57 couple the cell