Abstract
Fascin actin-bundling protein 1 (FSCN1) is a highly conserved actin-bundling protein that cross links F-actin microfilaments into tight, parallel bundles. Elevated FSCN1 levels have been reported in many types of human cancers and have been correlated with aggressive clinical progression, poor prognosis, and survival outcomes. The overexpression of FSCN1 in cancer cells has been associated with tumor growth, migration, invasion, and metastasis. Currently, FSCN1 is recognized as a candidate biomarker for multiple cancer types and as a potential therapeutic target. The aim of this study was to provide a brief overview of the FSCN1 gene and protein structure and elucidate on its actin-bundling activity and physiological functions. The main focus was on the role of FSCN1 and its upregulatory mechanisms and significance in cancer cells. Up-to-date studies on FSCN1 as a novel biomarker and therapeutic target for human cancers are reviewed. It is shown that FSCN1 is an unusual biomarker and a potential therapeutic target for cancer.
Highlights
Fascin actin-bundling protein 1 (FSCN1), known as fascin[1] or fascin, is a globular filamentous actin-binding protein of the fascin family.[1,2] By stabilizing actin bundles, FSCN1 supports a variety of cellular structures, including microspikes, filopodia, lamellipodia, and other actin-based protrusions underneath the plasma membrane.[3]
The ABS1 is formed by residues from the N and C termini of FSCN1 and includes the cleft formed by b-trefoil 1 and 4.17 This region includes a highly conserved site (Ser39) that can be phosphorylated by protein kinase C (PKC).[19,22,23]
Studies have shown that FSCN1 is expressed in many human cancer types
Summary
Fascin actin-bundling protein 1 (FSCN1), known as fascin[1] or fascin, is a globular filamentous actin-binding protein of the fascin family.[1,2] By stabilizing actin bundles, FSCN1 supports a variety of cellular structures, including microspikes, filopodia, lamellipodia, and other actin-based protrusions underneath the plasma membrane.[3]. FSCN1 expression is restricted to the neuronal, endothelial, mesenchymal, and dendritic cells[4] and is absent or at low levels in normal epithelial cells.[3] FSCN1 has been shown to be unusually expressed in transformed epithelial cells and many human cancers. This implies that it may functionally contribute toward cancer progression. We review the FSCN1 gene and protein structure, its regulation of actin-bundling activity, and its physiological functions. The ABS3 is a potential site that involves b-trefoil 3.17 all four b-trefoil domains of FSCN1 are involved in actin bundling
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