Unknown

Dataset Information

0

The Interactome of Palmitoyl-Protein Thioesterase 1 (PPT1) Affects Neuronal Morphology and Function.


ABSTRACT: 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.

SUBMITTER: Sapir T 

PROVIDER: S-EPMC6424868 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature

altmetric image

Publications

The Interactome of Palmitoyl-Protein Thioesterase 1 (PPT1) Affects Neuronal Morphology and Function.

Sapir Tamar T   Segal Michal M   Grigoryan Gayane G   Hansson Karin M KM   James Peter P   Segal Menahem M   Reiner Orly O  

Frontiers in cellular neuroscience 20190313


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  ...[more]

Similar Datasets

2019-11-08 | PXD006429 | Pride
| S-EPMC4701722 | biostudies-literature
| S-EPMC2839016 | biostudies-literature
| S-EPMC2881699 | biostudies-literature
| S-EPMC6775149 | biostudies-literature
| S-EPMC2914843 | biostudies-literature
| S-EPMC6739123 | biostudies-literature
2008-06-15 | E-GEOD-6678 | biostudies-arrayexpress
2007-01-09 | GSE6678 | GEO
| S-EPMC18274 | biostudies-literature