title: Subcellular localization specified by protein acylation and phosphorylation.
abstract: Modification of proteins by both lipophilic and hydrophilic moieties is widely documented. Here we present recent insights into how protein targeting is influenced by protein modification, with particular emphasis on dynamic regulation by fatty acylation and phosphorylation of proteins.
authors.affiliation: Harvard Medical School, Boston.
authors.forename: J
authors.initials: J
authors.lastname: Blenis
authors.forename: M D
authors.initials: MD
authors.lastname: Resh
mesh_terms: D000215:Acylation; D000818:Animals; D001692:Biological Transport; D002451:Cell Compartmentation; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D005227:Fatty Acids / Q000737:chemistry; D047908:Intracellular Signaling Peptides and Proteins; D008565:Membrane Proteins / Q000378:metabolism; D000076250:Myristoylated Alanine-Rich C Kinase Substrate; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism; D017479:Receptors, Platelet-Derived Growth Factor / Q000378:metabolism; D013347:Subcellular Fractions / Q000378:metabolism
chemical_list: D005227:Fatty Acids; D047908:Intracellular Signaling Peptides and Proteins; D008565:Membrane Proteins; D011506:Proteins; D000076250:Myristoylated Alanine-Rich C Kinase Substrate; D017479:Receptors, Platelet-Derived Growth Factor