Huntingtin-interacting protein 14, a palmitoyl transferase required for exocytosis and targeting of CSP to synaptic vesicles.

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The Journal of Cell Biology. 2007 Dec 31;179(7):1481-96. doi: 10.1083/jcb.200710061

Ohyama T, Verstreken P, Ly CV, Rosenmund T, Rajan A, Tien A, Haueter C, Schulze KL, Bellen HJ

Note: Research in this publication was not performed at Janelia.

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Abstract

Posttranslational modification through palmitoylation regulates protein localization and function. In this study, we identify a role for the Drosophila melanogaster palmitoyl transferase Huntingtin-interacting protein 14 (HIP14) in neurotransmitter release. hip14 mutants show exocytic defects at low frequency stimulation and a nearly complete loss of synaptic transmission at higher temperature. Interestingly, two exocytic components known to be palmitoylated, cysteine string protein (CSP) and SNAP25, are severely mislocalized at hip14 mutant synapses. Complementary DNA rescue and localization experiments indicate that HIP14 is required solely in the nervous system and is essential for presynaptic function. Biochemical studies indicate that HIP14 palmitoylates CSP and that CSP is not palmitoylated in hip14 mutants. Furthermore, the hip14 exocytic defects can be suppressed by targeting CSP to synaptic vesicles using a chimeric protein approach. Our data indicate that HIP14 controls neurotransmitter release by regulating the trafficking of CSP to synapses.

PMID: 18158335 [PubMed - indexed for MEDLINE]

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Huntingtin-interacting protein 14, a palmitoyl transferase required for exocytosis and targeting of CSP to synaptic vesicles.

Note: Research in this publication was not performed at Janelia.

Abstract

PMID: 18158335 [PubMed - indexed for MEDLINE]