UNDERSTANDING COVALENT MODIFICATIONS OF PROTEINS BY LIPIDS - WHERE CELL BIOLOGY AND BIOPHYSICS MINGLE

Much effort has beat expended on the in vitro characterization of enzy mes that covalently attach lipids to proteins. Less information is ava ilable about properties conferred on modified proteins by their attach ed lipid groups, but biophysical studies of simple model systems have begun to shed light on this issue. Recent evidence suggests that the s pecificity of lipid modifications may be dependent upon the intracellu lar compartmentalization of the lipid and protein substrates of lipida ting enzymes. The function and targeting of their lipidated products a ppear to be regulated dynamically through addition or subtraction of l ipid moieties, of her covalent or noncovalent modifications, as well a s several devices that at this point can only be inferred. This field of research illustrates the necessity of integrating cell-biological a nd biophysical perspectives.