The HECT domain ligase itch ubiquitinates endophilin and localizes to the trans-Golgi network and endosomal system
| Autor: | Antoine R. Ramjaun, Peter S. McPherson, Annie Angers |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
HECT domain
Endosome Ubiquitin-Protein Ligases Endocytic cycle Fluorescent Antibody Technique Golgi Apparatus NEDD4 macromolecular substances Endosomes Biochemistry SH3 domain Ubiquitin otorhinolaryngologic diseases Animals skin and connective tissue diseases Molecular Biology C2 domain DNA Primers biology Base Sequence Chemistry Cell Biology Ubiquitin ligase Cell biology Repressor Proteins COS Cells biology.protein Acyltransferases Subcellular Fractions |
| Zdroj: | The Journal of biological chemistry. 279(12) |
| ISSN: | 0021-9258 |
| Popis: | Endophilin A1 is an SH3 domain-containing protein functioning in membrane trafficking on the endocytic pathway. We have identified the E3 ubiquitin ligase itch/AIP4 as an endophilin A1-binding partner. Itch belongs to the Nedd4/Rsp5p family of proteins and contains an N-terminal C2 domain, four WW domains and a catalytic HECT domain. Unlike other Nedd4/Rsp5p family members, itch possesses a short proline-rich domain that mediates its binding to the SH3 domain of endophilin A1. Itch ubiquitinates endophilin A1 and the SH3/proline-rich domain interaction facilitates this activity. Interestingly, itch co-localizes with markers of the endosomal system in a C2 domain-dependent manner and upon EGF stimulation, endophilin A1 translocates to an EGF-positive endosomal compartment where it colocalizes with itch. Moreover, EGF treatment of cells stimulates endophilin A1 ubiquitination. We have thus identified endophilin A1 as a substrate for the endosome-localized ubiquitin ligase itch. This interaction may be involved in ubiquitin-mediated sorting mechanisms operating at the level of endosomes. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|