Methylation on leucine was first observed in 1999, the carboxyl methyltransferase, which is claimed to exclusively methylate the carboxyl group of the C-terminal leucine residue of the catalytic subunit of protein phosphatase 2A (Leu(309)), was purified from porcine brain. The cDNA encoding the human homologue was also cloned. The cDNA of this gene encodes for a protein of 334 amino acids with a calculated M(r) of 38 305 and a predicted pI of 5.72. Database screening reveals the presence of this protein in diverse phyla. Recent studies revealed that PP2A methylation is associated with "PP2A" dysfunction which has been linked to tau hyperphosphorylation, amyloidogenesis and synaptic deficits that are pathological hallmarks of this neurodegenerative disorder.

Reference
Pubmed: Sontag JM, Sontag E. Protein phosphatase 2A dysfunction in Alzheimer's disease Front Mol Neurosci. 2014 Mar 11;7:16. doi: 10.3389/fnmol.2014.00016. eCollection 2014.