The ATP-binding cassette (ABC) super-family of proteins is one of the largest families of proteins to have representatives in all living organisms from prokaryotes to humans. Superfamily members consist of an ABC motif that catalyzes ATP hydrolysis to power the transporter and a trans-membrane domain that regulates substrate selectivity. ABC transporters are responsible for the transport of a variety of molecules across cell membranes including lipids, cholesterol, peptides, bile salts, ions, steroids, and diverse drugs and have been shown to be critically involved in immune deficiency, cancer progression, cystic fibrosis, and cardio-vascular diseases.
The ABC genes are further grouped into 7 subfamilies (A-G). Prof. Wilfred Jefferies’s lab has discovered an essential role for an unusual member of this ancient and diverse superfamily – ABC family F member 1 (ABCF1). ABCF1 is the first ABC family member discovered that lacks a trans-membrane domain. It is primarily known as a regulator of translation induced by inflammation and has been associated with the pathophysiology of autoimmune pancreatitis and rheumatoid arthritis. However, the function of ABCF1 remains elusive.
