Tyrosine-based endocytic motifs stimulate oligomerization of AP-2 adaptor complexes |
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Authors: | Haucke Volker Krauss Michael |
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Institution: | aZentrum Biochemie and Molekulare Zellbiologie, Department of Biochemistry II, University of Göttingen, Göttingen/Germany |
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Abstract: | The clathrin adaptor complex AP-2 functions in the assembly of clathrin-coated vesicles at the plasma membrane where it serves to couple endocytic vesicle formation to the selection of membrane cargo proteins. Recent evidence suggests that binding of tyrosine-based endocytic sorting motifs may induce a conformational change within the AP-2 adaptor complex that could enhance its interaction with other cargo molecules and with the membrane. We report here that soluble tyrosine-based endocytic sorting motif peptides facilitate clathrin/AP-2 recruitment to liposomal membranes and induce adaptor oligomerization even in the absence of a lipid bilayer. These effects are specific for endocytic motifs of the type Yxxphi whereas peptides corresponding to NPxY- or di-leucine-containing sorting signals are ineffective. Our data may help to explain how the highly cooperative assembly of clathrin and adaptors could be linked to the selection of membrane cargo proteins. |
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Keywords: | Endocytic motif clathrin adaptor complex oligomerization AP-2 |
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