C met protein, also known as hepatocyte growth factor receptor (HGFR), is a receptor tyrosine kinase that plays a crucial role in a range of cellular activities including cell growth, survival, migration, and tissue regeneration. It belongs to the MET family of receptor tyrosine kinases and is encoded by the MET gene.
The c met protein is composed of an extracellular ligand-binding domain, a transmembrane domain, a juxtamembrane domain, a kinase domain, and a C-terminal tail. It is primarily activated by binding to its ligand, hepatocyte growth factor (HGF), which triggers a series of intracellular signaling cascades. Activation of c met promotes cell scattering, motility, and invasion, making it essential for embryonic development, tissue repair, and physiological processes such as wound healing.
Aberrant activation or overexpression of c met protein has been associated with various pathological conditions, including cancer. In cancer cells, c met often undergoes genetic alterations such as gene amplification, mutation, or overexpression, leading to dysregulated signaling pathways. This can result in enhanced tumor growth, metastasis, and resistance to therapies, making c met an attractive target for anticancer drugs.
In summary, c met protein is a receptor tyrosine kinase that regulates multiple cellular activities through activation by its ligand, HGF. It is crucial for normal cell growth and tissue regeneration but can contribute to cancer progression when dysregulated.
