AMPK is the major sensor of the cell’s energy status and co-ordinates energy reserves with biosynthetic activity by regulating mTORC1. AMPK activation occurs on the surface of the lysosome, where it co-localizes with mTORC1. Activated AMPK signals a need for catabolic activity and suppresses mTORC1. The recruitment of AMPK to the lysosomal surface requires the addition of a myristic acid lipid tail, that enables anchoring in the lysosomal membrane. Protein myristoylation is mediated by N-myristoyltransferase-1 (NMT1). Failure of NMT1 in RA T cells alters the intracellular trafficking of AMPK and prevents translocation to the cytoplasmic surface of the lysosome. One of the outcomes is unrestrained mTORC1 activation and a commitment of RA T cells to cellular proliferation and anabolic metabolism. AMPK, AMP-activated protein kinase; mTORC1, mechanistic target of rapamycin complex 1; NMT1, N-Myristoyltransferase-1.