title: Protein palmitoylation in signal transduction of hematopoietic cells.
abstract: The covalent attachment of palmitate to proteins can alter protein-lipid and protein-protein interactions thereby influencing protein function. Palmitoylation is a reversible post-translational modification. Thus, like protein phosphorylation, protein palmitoylation can function in activation-dependent signaling pathways. This review will provide an overview of the mechanisms and regulation of protein palmitoylation and focus on the role of palmitoylation in signal transduction pathways of lymphocytes and platelets.
authors.affiliation: Beth Israel Deaconess Medical Center, Harvard Medical School, Division of Hemostasis and Thrombosis, Department of Medicine, Boston, MA, 02215, USA. rflaumen@bidmc.harvard.edu
authors.forename: Robert
authors.initials: R
authors.lastname: Flaumenhaft
authors.forename: Derek S
authors.initials: DS
authors.lastname: Sim
mesh_terms: D000818:Animals; D001402:B-Lymphocytes / Q000378:metabolism*; D001792:Blood Platelets / Q000378:metabolism*; D001798:Blood Proteins / Q000378:metabolism*; D006801:Humans; D010169:Palmitic Acids / Q000378:metabolism*; D046188:Protein Modification, Translational; D015398:Signal Transduction; D013601:T-Lymphocytes / Q000378:metabolism*
chemical_list: D001798:Blood Proteins; D010169:Palmitic Acids