C-terminal protein lipidation

Definition

Target type: biologicalprocess

The covalent attachment of a lipid group to the carboxy-terminus of a protein. [GOC:jl]

C-terminal protein lipidation is a post-translational modification process that involves the attachment of a lipid molecule to the C-terminus of a protein. This modification plays a crucial role in various cellular processes, including protein targeting, membrane association, and signal transduction.

The process typically begins with the recognition of a specific C-terminal sequence by a lipid transferase enzyme. These enzymes, also known as translocases, catalyze the transfer of a lipid molecule from a donor lipid to the protein substrate. The lipid molecule can be a fatty acid, such as palmitate or myristate, or a prenyl group, such as farnesyl or geranylgeranyl.

The attachment of the lipid molecule to the protein occurs through a covalent bond. This bond can be formed via a thioester linkage (for fatty acylation), a thioether linkage (for prenylation), or an amide linkage (for myristoylation).

Once lipidated, the protein can undergo various fates. It may be targeted to specific cellular membranes, such as the plasma membrane, the endoplasmic reticulum, or the Golgi apparatus. This targeting is mediated by the lipid moiety, which interacts with the lipid bilayer of the membrane.

Alternatively, the lipidation may promote protein-protein interactions, facilitating the formation of signaling complexes or protein assemblies. The lipid moiety can serve as a docking site for other proteins, enabling them to interact and regulate cellular functions.

Overall, C-terminal protein lipidation is a highly regulated process that plays a pivotal role in cellular function. It is involved in a wide range of biological processes, including membrane trafficking, signal transduction, and protein-protein interactions. The specific lipid modification and the C-terminal sequence targeted are often highly specific and contribute to the diverse functions of lipidated proteins.'
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Proteins (3)

Compounds (11)