Geranylgeranylaatiota

Geranylgeranylaatio is a type of protein modification known as prenylation. It involves the covalent attachment of a geranylgeranyl pyrophosphate (GGPP) lipid molecule to a protein. This process is catalyzed by enzymes called geranylgeranyltransferases. Specifically, geranylgeranylaatio can occur at cysteine residues within a C-terminal consensus motif, typically CAAX or CCSS. The prenyl group is attached to the sulfur atom of the cysteine. This lipid modification plays a crucial role in protein localization, membrane association, and protein-protein interactions. Many proteins involved in signal transduction pathways, such as small GTPases, undergo geranylgeranylaatio. It is also important for the proper function of other proteins, including some nuclear lamins and ion channels. The geranylgeranyl group increases the hydrophobicity of the protein, facilitating its insertion into cellular membranes. Dysregulation of geranylgeranylaatio has been implicated in various diseases, highlighting its significance in cellular processes.