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Identification of far upstream element-binding protein-1 as an authentic Parkin substrate.

http://www.ncbi.nlm.nih.gov/pubmed/16672220

Aminoacyl-tRNA synthetase-interacting multifunctional protein type 2 was recently identified as an authentic substrate of the ubiquitin E3 ligase, parkin, a gene associated with autosomal recessive juvenile parkinsonism. Far upstream element-binding protein 1 is known to be degraded in an aminoacyl-tRNA synthetase interacting multifunctional protein type 2 dependent manner, which is crucial for lung cell maturation in early development. Therefore, we wondered whether far upstream element-binding protein 1 levels are altered in the absence of Parkin and in Parkinson disease. We herein report that far upstream element-binding protein 1 accumulates in Parkin knock-out mice, patients with autosomal recessive juvenile parkinsonism, sporadic Parkinson disease, and diffuse Lewy Body disease as well as the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine mouse model of Parkinson disease. Moreover, Parkin interacts with and ubiquitinates far upstream element-binding protein 1 facilitating its degradation through the ubiquitin proteasome system. Taken together, these results suggest that far upstream element-binding protein 1 is an authentic substrate of Parkin and that far upstream element-binding protein 1 might play an important role in development of Parkinson disease pathology along with aminoacyl-tRNA synthetase interacting multifunctional protein type 2.

Pubmed ID: 16672220 RIS Download

Mesh terms: Amino Acyl-tRNA Synthetases | Animals | Brain | DNA Helicases | DNA-Binding Proteins | Gene Expression Regulation | Humans | Mice | Mice, Knockout | Mice, Transgenic | Protein Binding | Tissue Distribution | Ubiquitin-Protein Ligases

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Associated grants

  • Agency: NINDS NIH HHS, Id: NS 38377
  • Agency: NINDS NIH HHS, Id: P50 NS038377

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