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The μ2 Subunit of the Clathrin Adaptor AP‐2 Binds to FDNPVY and YppØ Sorting Signals at Distinct Sites
Abstract
The endocytic sorting signal on the low‐density lipoprotein receptor for clathrin‐mediated internalization is the sequence FDNPVY in the receptor's cytosolic tail. We have used a combination of surface plasmon resonance and crosslinking with a photoactivated peptide probe to demonstrate the interaction between FDNPVY‐containing peptides and the μ2 chain of purified AP‐2 clathrin adaptors (the complexes responsible for plasma membrane sorting). We show that recognition of the FDNPVY signal is mediated by a binding site in the μ2‐subunit that is distinct from the site for the more general YppØ sorting signal, another tyrosine‐based sequence also recognized by μ2‐adaptin. These results suggest the possibility that low‐density lipoprotein receptor uptake may be modulated specifically and independently of other proteins in the clathrin pathway.
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Coated pits contain many potential binding partners for LDLR including AP2, PTB domain-containing adaptor proteins such as Dab2, and the clathrin heavy chain.
“In accordance with this mechanism, coated pits contain many potential binding partners for LDLR including AP2 (34), PTB domain-containing adaptor proteins such as Dab2 (12,28) and the clathrin heavy chain (35).”
From The Modular Adaptor Protein ARH Is Required for Low Density Lipoprotein (LDL) Binding and Internalization but Not for LDL Receptor Clustering in Coated Pits (2004) · cites this paper as [34]
The adaptor protein AP-2 binds other receptors that are internalized via clathrin-coated pits.
“The adaptor protein AP-2 has been shown to bind other receptors that are internalized via clathrin-coated pits”
From ARH Is a Modular Adaptor Protein That Interacts with the LDL Receptor, Clathrin, and AP-2 (2002) · cites this paper as [14]
Studies using plasmon resonance to test direct interactions between AP-2 and the FXNPXY motif of the LDLR tail have yielded contradictory results.
“studies using plasmon resonance to test for direct interactions between AP-2 and the FXNPXY motif of the LDLR tail have yielded contradictory results (13”
From ARH Is a Modular Adaptor Protein That Interacts with the LDL Receptor, Clathrin, and AP-2 (2002) · cites this paper as [14]
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Cited by
Sorted by citations
ARH Is a Modular Adaptor Protein That Interacts with the LDL Receptor, Clathrin, and AP-2
He, G., Gupta, S., Yi, M., Michaely, P., Hobbs, H. H., & Cohen, J. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208539200 · Cited by 232
Rajasekaran, S. A., Anilkumar, G., Oshima, E., Bowie, J. U., Liu, H., Heston, W., Bander, N. H., & Rajasekaran, A. K. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-11-0731 · Cited by 226
Michaely, P., Li, W.-P., Anderson, R. G. W., Cohen, J. C., & Hobbs, H. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405242200 · Cited by 66
Metadata
- Authors
- Boll, W., Rapoport, I., Brunner, C., Modis, Y., Prehn, S., & Kirchhausen, T.
- Venue
- Traffic
- Publisher
- Wiley
- Published
- 2002-07-16
- Volume
- 3
- Issue
- 8
- Pages
- 590-600
- ISSN
- 1398-9219
- 1600-0854
- Cited by
- 66
- References
- 0
- Language
- en
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