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Spartin activates atrophin-1-interacting protein 4 (AIP4) E3 ubiquitin ligase and promotes ubiquitination of adipophilin on lipid droplets by Christopher Hooper; Swamy S Puttamadappa; Zak Loring; Alexander Shekhtman; Joanna C Bakowska is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
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## Abstract ## Background Spartin protein is involved in degradation of epidermal growth factor receptor and turnover of lipid droplets and a lack of expression of this protein is responsible for hereditary spastic paraplegia type 20 (SPG20). Spartin is a multifunctional protein that associates with many cellular organelles, including lipid droplets. Recent studies showed that spartin interacts with E3 ubiquitin ligases that belong to the neural precursor cell-expressed developmentally downregulated gene (Nedd4) family, including atrophin-1-interacting protein 4 (AIP4/ITCH). However, the biological importance of the spartin-AIP4 interaction remains unknown. ## Results In this study, we show that spartin is not a substrate for AIP4 activity and that spartin's binding to AIP4 significantly increases self-ubiquitination of this E3 ligase, indicating that spartin disrupts the AIP4 autoinhibitory intramolecular interaction. Correspondingly, spartin has a seven times higher binding affinity to the WW region of AIP4 than the binding of the WW region has to the catalytic homologues of the E6-associated protein C-terminus (HECT) domain, as measured by enzyme-linked immunosorbent assay. We a
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It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- Christopher Hooper; Swamy S Puttamadappa; Zak Loring; Alexander Shekhtman; Joanna C Bakowska
- Publisher
- BioMed Central; Springer (Biomed Central Ltd.); [London]: BioMed Central, c2003-; Springer Science and Business Media LLC; Society for Mining, Metallurgy and Exploration Inc.; Research Square (ISSN 1741-7007)
- Published
- 2010
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)