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Structure and Function of Fbxo7/PARK15 in Parkinson's Disease.
- Source :
-
Current protein & peptide science [Curr Protein Pept Sci] 2017; Vol. 18 (7), pp. 715-724. - Publication Year :
- 2017
-
Abstract
- Fbxo7/PARK15 has well-defined roles, acting as part of a Skp1-Cul1-F box protein (SCF)- type E3 ubiquitin ligase and also having SCF-independent activities. Mutations within FBXO7 have been found to cause an early-onset Parkinson's disease, and these are found within or near to its functional domains, including its F-box domain (FBD), its proline rich region (PRR), and its ubiquitinlike domain (Ubl). We highlight recent advances in our understanding of Fbxo7 function in Parkinson's disease, with respect to these mutations and where they occur in the Fbxo7 protein. We hypothesize that many of Fbxo7 functions contribute to its role in PD pathogenesis.<br /> (Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.org.)
- Subjects :
- Animals
Drosophila melanogaster genetics
Drosophila melanogaster metabolism
F-Box Proteins chemistry
F-Box Proteins metabolism
Gene Expression
Humans
Neurons metabolism
Neurons pathology
Parkinson Disease metabolism
Parkinson Disease pathology
Protein Domains
SKP Cullin F-Box Protein Ligases chemistry
SKP Cullin F-Box Protein Ligases metabolism
Structure-Activity Relationship
Ubiquitination
F-Box Proteins genetics
Mutation
Parkinson Disease genetics
SKP Cullin F-Box Protein Ligases genetics
Subjects
Details
- Language :
- English
- ISSN :
- 1875-5550
- Volume :
- 18
- Issue :
- 7
- Database :
- MEDLINE
- Journal :
- Current protein & peptide science
- Publication Type :
- Academic Journal
- Accession number :
- 26965690
- Full Text :
- https://doi.org/10.2174/1389203717666160311121433