The solute carrier family 27 of fatty acid transport protein is also known as FATPs. Although FATPs have sequence similarity, these proteins are differentially expressed in a variety of tissues and cell types (liver, skeletal muscle, adipose tissue, heart, intestine, skin, and endothelial cells, etc.). Research of gain- and loss-of-function demonstrate the categorical role of FATPs in the regulation of LCFA uptake. However, the precise mechanism by which FATPs play a role in LCFA uptake remains controversial. FATPs have been proposed as direct transporters of LCFA, as enzymes that activate LCFA by intrinsic acyl-CoA synthetase (ACS) activity, or as bifunctional proteins with independent transport and enzymatic activity. FATP1 (SLC27A1) is the first FATP identified based on its ability to increase LCFA uptake when overexpressed in cells. In addition to their role in fatty acid uptake, it is also shown that FATPs display ACS activity. The ACS enzyme catalyzes the conversion of LCFA to acyl-CoA thioester to activate LCFA. Studies examining the subcellular localization of FATPs support the role of the proteins in fatty acid uptake and activation. FATP can be present in both the plasma membrane and intracellular spaces. The identification of FATPs and cytoplasm in the plasma membrane confirmed their roles as bifunctional proteins in the fatty acid uptake and activation.
Fig.1 FATP expression pattern in vivo. (Anderson, 2013)
The SLC27 gene family is comprised of six members, SLC27A1-SLC27A6, which encode FATP1- FATP6.
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