Lipideren

Lipideren is a biochemical process by which lipid groups are covalently attached to molecules, most commonly proteins, resulting in lipidation. This post-translational modification alters protein hydrophobicity and promotes association with cellular membranes or lipophilic compartments. Lipideren occurs in many organisms, and its extent and specific forms influence protein localization, stability, and interactions.

Several major forms are described. N-myristoylation attaches a myristoyl group to a glycine at the N-terminus following removal of the initial methionine. S-palmitoylation adds palmitoyl groups to cysteine residues via thioester bonds. Prenylation attaches farnesyl or geranylgeranyl groups to a cysteine near the C-terminus within a CAAX motif. GPI anchoring transfers a glycosylphosphatidylinositol anchor to a terminal protein residue, relocating it to the outer leaflet of the plasma membrane.

Biological roles include membrane targeting and microdomain localization, regulation of protein–protein interactions, and control of trafficking between organelles. Lipidated proteins can cycle between cytosol and membranes, or be stably anchored. Lipideren also influences protein turnover and signaling within pathways such as growth, apoptosis, or immune recognition.

Enzymes mediating lipideren comprise N-myristoyltransferases, palmitoyltransferases (e.g., the DHHC family), and prenyltransferases, as well as enzymes of GPI-anchor biosynthesis. Lipid donors include myristoyl-CoA, palmitoyl-CoA, and prenyl pyrophosphate derivatives. Changes in lipidation patterns can affect disease processes and are targets for therapeutic intervention in cancer, infectious diseases, and neurological disorders.

Detection and study rely on biochemical labeling, mass spectrometry, and imaging approaches. Experimental manipulation—such as enzyme knockouts or mutational disruption of lipidation motifs—helps reveal functional consequences. While lipideren is essential for many cellular functions, its precise roles vary by organism and protein context.