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AP-2 Recruitment to Synaptotagmin Stimulated by Tyrosine-Based Endocytic Motifs
Abstract
Clathrin-mediated endocytosis is initiated by the recruitment of the clathrin adaptor protein AP-2 to the plasma membrane where the membrane protein synaptotagmin is thought to act as a docking site. AP-2 also interacts with endocytic motifs present in other cargo proteins. Peptides with a tyrosine-based endocytic motif stimulated binding of AP-2 to synaptotagmin and enhanced AP-2 recruitment to the plasma membrane of neuronal and non-neuronal cells. This suggests a mechanism by which nucleation of clathrin-coated pits is stimulated by the loading of cargo proteins.
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Cited by
Molecular mechanism and physiological functions of clathrin-mediated endocytosis
McMahon, H. T., & Boucrot, E. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3151 · Cited by 2,223
Signals for Sorting of Transmembrane Proteins to Endosomes and Lysosomes
Bonifacino, J. S., & Traub, L. M. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161800 · Cited by 2,040
Essential Role of Phosphoinositide Metabolism in Synaptic Vesicle Recycling
Cremona, O., Di Paolo, G., Wenk, M. R., Lüthi, A., Kim, W. T., Takei, K., Daniell, L., Nemoto, Y., Shears, S. B., Flavell, R. A., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)81649-9 · Cited by 834
Kirchhausen, T. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.699 · Cited by 560
Kirchhausen, T. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35043117 · Cited by 560
Metadata
- Authors
- Haucke, V., & Camilli, P. D.
- Venue
- Science
- Published
- 1999-08-20
- Volume
- 285
- Issue
- 5431
- Pages
- 1268-1271
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1994128601
- Cited by
- 193
- References
- 0
- FWCI
- 6.68
- Type
- journal article
- Language
- en
- Open access
- closed
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- Haucke, V., & Camilli, P. D. (1999). AP-2 Recruitment to Synaptotagmin Stimulated by Tyrosine-Based Endocytic Motifs. Science. https://doi.org/10.1126/science.285.5431.1268
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