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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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) Vol. 269; no. 5232; pp. 1872 - 1875
Main Authors: Ohno, Hiroshi, Stewart, Jay, Fournier, Marie-Christine, Bosshart, Herbert, Rhee, Ina, Miyatake, Shoichiro, Saito, Takashi, Gallusser, Andreas, Kirchhausen, Tomas, Bonifacino, Juan S.
Format: Journal Article
Language:English
Published: 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
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ISSN:0036-8075, 1095-9203
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Summary: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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ISSN:0036-8075
1095-9203
DOI:10.1126/science.7569928