Putting proteins in their place: Palmitoylation in Huntington disease and other neuropsychiatric diseases

@article{Young2012PuttingPI,
  title={Putting proteins in their place: Palmitoylation in Huntington disease and other neuropsychiatric diseases},
  author={F. B. Young and S. Butland and S. Sanders and L. Sutton and M. Hayden},
  journal={Progress in Neurobiology},
  year={2012},
  volume={97},
  pages={220-238}
}
  • F. B. Young, S. Butland, +2 authors M. Hayden
  • Published 2012
  • Biology, Medicine
  • Progress in Neurobiology
    • Post-translational modification of proteins by the lipid palmitate is critical for protein localization and function. Palmitoylation is regulated by the opposing enzymes palmitoyl acyltransferases (PATs) and acyl protein thioesterases, which add and remove palmitate from proteins, respectively. Palmitoylation is particularly important for a number of processes including neuronal development and synaptic activity in the central nervous system. Dysregulated palmitoylation contributes to… CONTINUE READING
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    The palmitoyl acyltransferase HIP 14 shares a high proportion of interactors with huntingtin : implications for a role in the pathogenesis of Huntington ’ s disease
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    Curation of the Mammalian Palmitoylome Indicates a Pivotal Role for Palmitoylation in Diseases and Disorders of the Nervous System and Cancers
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    Huntingtin interacting proteins 14 and 14-like are required for chorioallantoic fusion during early placental development.
    • 3
    Insights Into Protein S-Palmitoylation in Synaptic Plasticity and Neurological Disorders: Potential and Limitations of Methods for Detection and Analysis
    • 14
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    Identification of Binding Sites in Huntingtin for the Huntingtin Interacting Proteins HIP14 and HIP14L
    • 18
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    Protein S-palmitoylation and cancer.
    • 63
    Targeting protein palmitoylation: selective inhibitors and implications in disease
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    Hip14l-deficient mice develop neuropathological and behavioural features of Huntington disease.
    • 53
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