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From Proteopedia

1 Lipid Scramblase nhTMEM16

Lipid Scramblase nhTMEM16

Structure

The lipid scramblase nhTMEM16 protein is a homo dimer, meaning its primary structure is composed of two identical chains. The defining feature of this protein is its calcium-activated chloride channels. The binding sites for these Ca2+ ions are located in the hydrophobic center of the molecule. These parts can be seen below, under the "structural highlights" section of this page.

Function

TMEM16 proteins are responsible for the eventual activation of platelets which is important for blood clotting. They are also responsible for the movement of phospholipids across the bilayer and even play an important role in apoptosis.

Calcium-activated chloride channels are an important element in many mammalian excitable cells. They facilitate the passive diffusion of chlorine ions in and out of the cell, which helps regulate the membrane potential.

Disease

Scott syndrome is a rare human disease caused by a mutation that affects TMEM16 proteins and results in the inability of platelets and other hematopoietic cells to bring phosphatidylserine to the surface for proper coagulation.

Relevance

Though lipid scramblase nhTMEM16 is most significant for those with Scotts syndrome, it is highly important in all organisms due to its role in apoptosis. If it were not able to enable cell death, cancerous cell behavior would be highly prevalent and even more dangerous.