Fodrin

Fodrin is a protein that is found in the cytoskeleton of eukaryotic cells. It is also known as spectrin in erythrocytes (red blood cells). Fodrin is a crucial component of the cytoskeleton, providing structural support and facilitating cell shape changes.

Structure[edit | edit source]

Fodrin is a tetramer composed of two alpha and two beta subunits. The alpha and beta subunits are similar in structure, each consisting of a series of spectrin repeats. These repeats are composed of three alpha-helices arranged in a coiled-coil configuration. The alpha subunit of fodrin is slightly larger than the beta subunit, with a molecular weight of approximately 280 kDa compared to the beta subunit's 220 kDa.

Function[edit | edit source]

Fodrin plays a critical role in maintaining the shape and flexibility of cells. It forms a mesh-like network beneath the cell membrane, providing structural support and facilitating changes in cell shape. Fodrin is also involved in various cellular processes, including cell division, cell adhesion, and cell signaling. It interacts with other proteins, such as ankyrin, to anchor the cytoskeleton to the cell membrane.

Clinical significance[edit | edit source]

Mutations in the genes encoding the alpha and beta subunits of fodrin can lead to a variety of diseases. For example, mutations in the alpha fodrin gene have been associated with autoimmune diseases, such as Sjögren's syndrome and systemic lupus erythematosus. Mutations in the beta fodrin gene can lead to hereditary spherocytosis, a condition characterized by anemia, jaundice, and an enlarged spleen.