Tyrosine kinase

Tyrosine kinase is an enzyme that can transfer a phosphate group from ATP to a protein in a cell. It functions as an "on" or "off" switch in many cellular functions. Tyrosine kinases are a subclass of protein kinase.

The phosphate group is attached to the amino acid tyrosine on the protein. This process is called phosphorylation. Phosphorylation of proteins by kinases is an important mechanism in communicating signals within a cell (signal transduction) and regulating cellular activity, such as cell division.

Tyrosine kinases have been shown to be involved in many types of cancer and in conditions such as inflammation and immune diseases.

Function

Tyrosine kinases function in many cellular processes, including cell growth and division, cell movement, cell death, and cell shape. They act as molecular switches, and they help to control these processes by adding phosphate groups to other molecules. This process is called phosphorylation.

Types

There are two types of tyrosine kinases: receptor tyrosine kinases (RTKs), which are associated with cell membranes, and non-receptor tyrosine kinases, which are found in the cytoplasm of the cell.

Role in disease

Tyrosine kinases have been found to be important in many types of cancer. They are also involved in inflammation and immune diseases.

See also

• Protein kinase
• Phosphorylation
• Signal transduction
• Cancer
• Inflammation
• Immune diseases

References

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