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Peter James

Peter James

Professor

Peter James

The interactome of palmitoyl-protein thioesterase 1 (PPT1) affects neuronal morphology and function

Author

  • Tamar Sapir
  • Michal Segal
  • Gayane Grigoryan
  • Karin M. Hansson
  • Peter James
  • Menahem Segal
  • Orly Reiner

Summary, in English

Palmitoyl-protein thioesterase 1 (PPT1) is a depalmitoylation enzyme that is mutated in cases of neuronal ceroid lipofuscinosis (NCL). The hallmarks of the disease include progressive neurodegeneration and blindness, as well as seizures. In the current study, we identified 62 high-confident PPT1-binding proteins. These proteins included a self-interaction of PPT1, two V-type ATPases, calcium voltage-gated channels, cytoskeletal proteins and others. Pathway analysis suggested their involvement in seizures and neuronal morphology. We then proceeded to demonstrate that hippocampal neurons from Ppt1−/− mice exhibit structural deficits, and further investigated electrophysiology parameters in the hippocampi of mutant mice, both in brain slices and dissociated postnatal primary cultures. Our studies reveal new mechanistic features involved in the pathophysiology of this devastating neurodegenerative disease.

Department/s

  • Department of Immunotechnology

Publishing year

2019-01-29

Language

English

Publication/Series

Frontiers in Cellular Neuroscience

Volume

13

Document type

Journal article

Publisher

Frontiers Media S. A.

Topic

  • Neurosciences

Keywords

  • Hippocampal neurons
  • Mass-spectrometry
  • Palmitoyl-protein thioesterase 1
  • Palmitoylation
  • PPT1

Status

Published

ISBN/ISSN/Other

  • ISSN: 1662-5102