Protein farnesyltransferase

From WikiMD's Food, Medicine & Wellness Encyclopedia

Protein Farnesyltransferase (PFT) is an enzyme that plays a crucial role in the post-translational modification of proteins. This enzyme is responsible for the addition of a farnesyl group to the C-terminus of a protein, a process known as farnesylation.

Function[edit | edit source]

Protein Farnesyltransferase catalyzes the transfer of a farnesyl group from farnesyl pyrophosphate to the cysteine residue of a protein. This modification is necessary for the proper localization and function of the protein. Farnesylation is particularly important for the function of several G proteins, which are involved in transmitting signals within cells.

Structure[edit | edit source]

Protein Farnesyltransferase is a heterodimer, composed of two different subunits. The alpha subunit is responsible for binding the farnesyl pyrophosphate, while the beta subunit recognizes the specific protein to be farnesylated.

Clinical significance[edit | edit source]

Abnormalities in the function of Protein Farnesyltransferase can lead to a variety of diseases. For example, mutations in the genes encoding the subunits of this enzyme have been associated with Hutchinson-Gilford Progeria Syndrome, a rare genetic disorder characterized by rapid aging. In addition, inhibitors of Protein Farnesyltransferase are being investigated as potential treatments for cancer, as the farnesylation of certain proteins is necessary for the growth and survival of cancer cells.

See also[edit | edit source]




Wiki.png

Navigation: Wellness - Encyclopedia - Health topics - Disease Index‏‎ - Drugs - World Directory - Gray's Anatomy - Keto diet - Recipes

Search WikiMD


Ad.Tired of being Overweight? Try W8MD's physician weight loss program.
Semaglutide (Ozempic / Wegovy and Tirzepatide (Mounjaro) available.
Advertise on WikiMD

WikiMD is not a substitute for professional medical advice. See full disclaimer.

Credits:Most images are courtesy of Wikimedia commons, and templates Wikipedia, licensed under CC BY SA or similar.

Contributors: Prab R. Tumpati, MD