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

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

Authors

  • Ko HS
  • Kim SW
  • Sriram SR
  • Dawson VL
  • Dawson TM

Journal

The Journal of biological chemistry

Publication Data

June 16, 2006

Associated Grants

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

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