Редактирование: USP15

Ubiquitin carboxyl-terminal hydrolase 15 (EC 3.4.19.12) (Deubiquitinating enzyme 15) (Ubiquitin thioesterase 15) (Ubiquitin-specific-processing protease 15) (Unph-2) (Unph4) [KIAA0529]

==Publications==

{{medline-entry
|title=Deficiency of parkin and [[PINK1]] impairs age-dependent mitophagy in [i]Drosophila[/i].
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/29809156
|abstract=Mutations in the genes for [[PINK1]] and parkin cause Parkinson's disease. [[PINK1]] and parkin cooperate in the selective autophagic degradation of damaged mitochondria (mitophagy) in cultured cells. However, evidence for their role in mitophagy in vivo is still scarce. Here, we generated a [i]Drosophila[/i] model expressing the mitophagy probe mt-Keima. Using live mt-Keima imaging and correlative light and electron microscopy (CLEM), we show that mitophagy occurs in muscle cells and dopaminergic neurons in vivo, even in the absence of exogenous mitochondrial toxins. Mitophagy increases with aging, and this age-dependent rise is abrogated by [[PINK1]] or parkin deficiency. Knockdown of the [i]Drosophila[/i] homologues of the deubiquitinases [[USP15]] and, to a lesser extent, [[USP30]], rescues mitophagy in the parkin-deficient flies. These data demonstrate a crucial role for parkin and [[PINK1]] in age-dependent mitophagy in [i]Drosophila[/i] in vivo.
|mesh-terms=* Aging
* Animals
* Autophagy
* Dopaminergic Neurons
* Drosophila Proteins
* Drosophila melanogaster
* Mitochondria
* Mitophagy
* Muscle, Skeletal
* Protein-Serine-Threonine Kinases
* Ubiquitin-Protein Ligases
|keywords=* D. melanogaster
* Parkinson's disease
* USP15
* USP30
* aging
* autophagy
* cell biology
* human biology
* medicine
* mitochondria
|full-text-url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6008047
}}