The U-box ligase carboxyl-terminus of Hsc 70-interacting protein ubiquitylates Epsin
| Autor: | John P. O'Bryan, Stephanie L.H. Miller, Robert P. Mohney, Yoav E. Timsit |
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| Rok vydání: | 2005 |
| Předmět: |
Epsin
Ubiquitin-Protein Ligases Endocytic cycle Biophysics Vesicular Transport Proteins Endocytosis Kidney Biochemistry Cell Line Structure-Activity Relationship Ubiquitin Humans HSP70 Heat-Shock Proteins Molecular Biology chemistry.chemical_classification DNA ligase Binding Sites biology Chemistry HSC70-INTERACTING PROTEIN HSC70 Heat-Shock Proteins Signal transducing adaptor protein Cell Biology Cell biology Ubiquitin ligase Adaptor Proteins Vesicular Transport biology.protein Protein Binding |
| Zdroj: | Biochemical and biophysical research communications. 328(2) |
| ISSN: | 0006-291X |
| Popis: | Epsin is an endocytic adaptor protein involved in the regulation of clathrin-dependent endocytosis. We and others have demonstrated that Epsin is ubiquitylated in cells and requires its ubiquitin interacting motifs (UIMs) for this modification. To further elucidate the mechanism of Epsin ubiquitylation, we initiated studies to identify the E3 ligase(s) that modifies Epsin. In this study, we discovered that the U-box ubiquitin ligase carboxyl-terminus of Hsc70 interacting protein (CHIP) ubiquitylated Epsin. Using an in vitro ubiquitylation assay, we demonstrate that CHIP specifically ubiquitylated Epsin in a UIM-dependent manner. Furthermore, overexpression of CHIP in cells increased Epsin ubiquitylation also in a UIM-dependent manner. Together, these data provide evidence that CHIP functions to ubiquitylate the endocytic protein Epsin. |
| Databáze: | OpenAIRE |
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