Dynamic palmitoylation of neuromodulin (GAP-43) in cultured rat cerebellar neurons and mouse N1E-115 cells.
We conducted pulse-chase and metabolic labeling experiments to determine directly whether palmitoylation of neuromodulin in neurons is dynamic, and if acylation is regulated. The rates of turnover of neuromodulin protein and associated palmitoyl groups were quantified using cultured cerebellar granule neurons and the neuronal cell line N1E-115. The half-life of [3H]palmitate bound to neuromodulin was approximately 5 h, whereas the half-life of the [35S]methionine-labeled neuromodulin was greater than 50 h. Metabolic and pulse-chase labeling experiments were carried out in the presence of various activators of cellular signaling pathways. Our data indicate that dynamic acylation and deacylation of neuromodulin in neurons are constitutive and are not regulated by G protein activation or other signals that control growth cone dynamics.
Baker
L P
LP
Department of Pharmacology, University of Washington, Seattle 98195-7280, USA.
Storm
D R
DR
D000215:Acylation; D000818:Animals; D002460:Cell Line; D002478:Cells, Cultured; D002531:Cerebellum / Q000166:cytology / Q000378:metabolism*; D019922:GAP-43 Protein / Q000378:metabolism*; D019204:GTP-Binding Proteins / Q000378:metabolism; D006207:Half-Life; D051379:Mice; D009474:Neurons / Q000378:metabolism*; D019308:Palmitic Acid / Q000378:metabolism*; D051381:Rats; D015398:Signal Transduction / Q000502:physiology*
D019922:GAP-43 Protein; D019308:Palmitic Acid; D019204:GTP-Binding Proteins