The lipid moieties added to proteins can be either fatty acyl or polyisoprenyl groups, and the modifications typically occur on the nucleophilic side chains of proteins (e.g., cysteine, serine, and lysine) and the NH 2 group at the N-termini of proteins ( Figure 1). The effects of protein lipidation on cellular function are achieved by regulating protein–membrane interactions, and perhaps somewhat surprising, protein–protein interactions, protein stability, and enzymatic activities. Lipidation occurs on numerous proteins and regulates many aspects of physiology. ![]() These modifications are the focus of this review. 2 Another widely observed interaction strategy is the covalent modification of proteins by lipid molecules. For example, some pleckstrin homology domains recognize specific phosphoinositides, 1 and blood clotting factors recognize phosphatidylserine, which is found only in the inner leaflet of the plasma membrane. Certain proteins have evolved to bind specifically to certain lipid molecules. These functions are achieved through two strategies. Not surprisingly, nature also uses lipids to control and regulate membrane–protein interactions. ![]() Cell signaling and membrane trafficking rely on proteins that are secreted into the environment, embedded in cellular membranes, and reversibly associated with membranes. This confinement of cellular materials by cellular membrane structures necessitates cellular communication (i.e., cell signaling and membrane trafficking) with the extracellular environment and among cellular membrane organelles. Lipids are essential molecules that compose cellular membranes, which provide the barriers and boundaries needed for cells to survive and proliferate.
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