Neuronal activity moves protein palmitoylation into the synapse.
Many neuronal proteins undergo lipid modification that regulates their function and subcellular localization. One such modification is palmitoylation, which is mediated by a large class of protein palmitoyl acyltransferases (PATs). Now, a paper in this issue (Noritake et al. 2009. J. Cell Biol. doi:10.1083/jcb.200903101) demonstrates that the localization of the PAT DHHC2 is regulated by neuronal activity and thereby selectively controls the palmitoylation and subsequent accumulation of specific proteins in the synapse.
Dalva
Matthew B
MB
Department of Neuroscience, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA. dalva@mail.med.upenn.edu
D000123:Acetyltransferases / Q000737:chemistry / Q000378:metabolism; D003712:Dendrites / Q000201:enzymology; D000076122:Disks Large Homolog 4 Protein; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000378:metabolism*; D054878:Lipoylation; D008565:Membrane Proteins / Q000378:metabolism*; D008954:Models, Biological; D009474:Neurons / Q000378:metabolism*; D021381:Protein Transport; D013569:Synapses / Q000378:metabolism*
D000076122:Disks Large Homolog 4 Protein; C501449:Dlg4 protein, rat; D047908:Intracellular Signaling Peptides and Proteins; D008565:Membrane Proteins; D000123:Acetyltransferases; C062782:protein acyltransferase