Glutamate oxaloacetate transaminase 2 (GOT2) (FABPpm)

Plasma membrane fatty acid-binding protein (FABPpm) is a 43-kDa peripheral membrane protein that is identical to the mitochondrial isoform of aspartate aminotransferase (mAST), encoded by the GOT2 gene (UniProt P00505). While its primary enzymatic role occurs within the mitochondria as part of the malate-aspartate shuttle, it is also localized to the plasma membrane where it functions as a transporter for long-chain fatty acids (LCFAs) (Glatz et al., 2010). FABPpm facilitates the initial binding and translocation of fatty acids across the lipid bilayer, often working in coordination with other transporters like CD36 to regulate lipid flux (Bonen et al., 2004). In metabolic disorders such as obesity and type 2 diabetes, FABPpm expression and its translocation to the cell surface are often increased in skeletal muscle and liver, leading to enhanced fatty acid uptake and contributing to lipotoxicity and insulin resistance (Chabowski et al., 2007). Because of its role in lipid oversupply, it is considered a potential therapeutic target for metabolic syndrome, although its dual role in essential mitochondrial metabolism poses a significant challenge for drug specificity. Experimental inhibitors like sulfo-N-succinimidyl oleate (SSO) have demonstrated that blocking FABPpm can significantly reduce LCFA uptake in various tissues, providing a proof-of-concept for metabolic intervention (Luiken et al., 1999).

Other names

Plasma membrane fatty acid-binding proteinMitochondrial aspartate aminotransferasemASTAspartate aminotransferase 2Fatty acid-binding protein, plasma membrane-associated

Inhibition of long-chain fatty acid (LCFA) uptake across the plasma membrane (Luiken et al., 1999)