Interaction of Tyrosine-Based Sorting Signals with Clathrin-Associated Proteins
Tyrosine-based signals within the cytoplasmic domain of integral membrane proteins mediate clathrin-dependent protein sorting in the endocytic and secretory pathways. A yeast two-hybrid system was used to identify proteins that bind to tyrosine-based signals. The medium chains ($\mu_1$ and $\mu_2$)...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) Jg. 269; H. 5232; S. 1872 - 1875 |
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| Hauptverfasser: | , , , , , , , , , |
| Format: | Journal Article |
| Sprache: | Englisch |
| Veröffentlicht: |
Washington, DC
American Society for the Advancement of Science
29.09.1995
American Association for the Advancement of Science The American Association for the Advancement of Science |
| Schlagworte: | |
| ISSN: | 0036-8075, 1095-9203 |
| Online-Zugang: | Volltext |
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| Zusammenfassung: | Tyrosine-based signals within the cytoplasmic domain of integral membrane proteins mediate clathrin-dependent protein sorting in the endocytic and secretory pathways. A yeast two-hybrid system was used to identify proteins that bind to tyrosine-based signals. The medium chains ($\mu_1$ and $\mu_2$) of two clathrin-associated protein complexes (AP-1 and AP-2, respectively) specifically interacted with tyrosine-based signals of several integral membrane proteins. The interaction was confirmed by in vitro binding assays. Thus, it is likely that the medium chains serve as signal-binding components of the clathrin-dependent sorting machinery. |
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| Bibliographie: | SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 14 ObjectType-Article-2 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
| ISSN: | 0036-8075 1095-9203 |
| DOI: | 10.1126/science.7569928 |