Abstract：
:In neurons, posttranslational modification by palmitate regulates the trafficking and function of signaling molecules, neurotransmitter receptors, and associated synaptic scaffolding proteins. However, the enzymatic machinery involved in protein palmitoylation has remained elusive. Here, using biochemical assays, we show that huntingtin (htt) interacting protein, HIP14, is a neuronal palmitoyl transferase (PAT). HIP14 shows remarkable substrate specificity for neuronal proteins, including SNAP-25, PSD-95, GAD65, synaptotagmin I, and htt. Conversely, HIP14 is catalytically invariant toward paralemmin and synaptotagmin VII. Exogenous HIP14 enhances palmitoylation-dependent vesicular trafficking of several acylated proteins in both heterologous cells and neurons. Moreover, interference with endogenous expression of HIP14 reduces clustering of PSD-95 and GAD65 in neurons. These findings define HIP14 as a mammalian palmitoyl transferase involved in the palmitoylation and trafficking of multiple neuronal proteins.
journal_name
Neuronjournal_title
Neuronauthors
Huang K,Yanai A,Kang R,Arstikaitis P,Singaraja RR,Metzler M,Mullard A,Haigh B,Gauthier-Campbell C,Gutekunst CA,Hayden MR,El-Husseini Adoi
10.1016/j.neuron.2004.11.027subject
Has Abstractpub_date
2004-12-16 00:00:00pages
977-86issue
6eissn
0896-6273issn
1097-4199pii
S0896627304007500journal_volume
44pub_type
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