FLT4 Regulates TGF-β Signaling Pathway and Impacts on Cell Survival and Differentiation

Target Name: FLT4

NCBI ID: G2324

FLT4

FLT4 Regulates TGF-β Signaling Pathway and Impacts on Cell Survival and Differentiation

FLT4 (Focal Adhesion Molecule (FAIM) 4) is a protein that is expressed in various tissues and cell types in the human body. It is a member of the FAIM family, which includes proteins that are involved in cell-cell adhesion, migration, and invasion. FLT4 has been shown to be involved in the development and progression of several diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. As a result, FLT4 has become a focus of interest for researchers who are seeking new potential drug targets or biomarkers.

One of the key features of FLT4 is its ability to form focal adhesion, a type of cell-cell adhesion that is essential for the development and maintenance of tissues and organs. Focal adhesion is a complex process that involves the interaction between several proteins, including FLT4. These proteins help to regulate the movement of cells, ensure that they stick together to form tissues and organs, and facilitate the formation of new blood vessels.

FLT4 has been shown to be involved in the regulation of several key signaling pathways that are involved in cell growth, differentiation, and survival. One of the most well-studied of these pathways is the TGF-β pathway, which is involved in the regulation of cell growth, differentiation, and survival. TGF-β is a cytokine that is involved in the development of tissues and organs, and it is activated by FLT4.

FLT4 has been shown to play a key role in the regulation of TGF-β signaling pathway. It is a negative regulator of TGF-β, which means that it works to inhibit the activity of TGF-β. This is important because TGF-β is involved in the development and maintenance of tissues and organs, and it is often involved in the development of cancer. By inhibiting TGF-β, FLT4 may be able to reduce the risk of cancer.

Another key aspect of FLT4's role in TGF-β signaling pathway is its ability to regulate the activity of several proteins that are involved in the TGF-β pathway. These proteins include SMAD, KLF1, and TGF-β2. SMAD is a transcription factor that is involved in the regulation of gene expression, and KLF1 is a RNA polymerase that is involved in the regulation of gene expression. TGF-β2 is a cytokine that is involved in the regulation of cell growth and differentiation.

FLT4 has also been shown to be involved in the regulation of several other signaling pathways that are important for cell survival and differentiation. These include the PI3K/AKT signaling pathway, the NF-kappa-B signaling pathway, and the T-cell signaling pathway.

In addition to its role in TGF-β signaling pathway, FLT4 has also been shown to be involved in the regulation of several important cellular processes that are involved in cell survival and differentiation. These include cell adhesion, migration, and the regulation of cell apoptosis.

FLT4 has been shown to play a key role in the regulation of cell adhesion, which is the process by which cells stick together to form tissues and organs. This is important because cell adhesion is involved in the development and maintenance of tissues and organs, and it is often involved in the development of cancer. By regulating cell adhesion, FLT4 may be able to reduce the risk of cancer.

FLT4 has also been shown to play a key role in the regulation of cell migration, which is the process by which cells move from one location to another. This is important because cell migration is involved in the development and maintenance of tissues and organs, and it is often involved in the development of cancer. By regulating cell migration, FLT4 may be able to

Protein Name: Fms Related Receptor Tyrosine Kinase 4

Functions: Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFC and VEGFD, and plays an essential role in adult lymphangiogenesis and in the development of the vascular network and the cardiovascular system during embryonic development. Promotes proliferation, survival and migration of endothelial cells, and regulates angiogenic sprouting. Signaling by activated FLT4 leads to enhanced production of VEGFC, and to a lesser degree VEGFA, thereby creating a positive feedback loop that enhances FLT4 signaling. Modulates KDR signaling by forming heterodimers. The secreted isoform 3 may function as a decoy receptor for VEGFC and/or VEGFD and play an important role as a negative regulator of VEGFC-mediated lymphangiogenesis and angiogenesis. Binding of vascular growth factors to isoform 1 or isoform 2 leads to the activation of several signaling cascades; isoform 2 seems to be less efficient in signal transduction, because it has a truncated C-terminus and therefore lacks several phosphorylation sites. Mediates activation of the MAPK1/ERK2, MAPK3/ERK1 signaling pathway, of MAPK8 and the JUN signaling pathway, and of the AKT1 signaling pathway. Phosphorylates SHC1. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Promotes phosphorylation of MAPK8 at 'Thr-183' and 'Tyr-185', and of AKT1 at 'Ser-473'

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