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Clathrin-binding proteins: Got a motif? Join the network!
Abstract
Clathrin plays a key function in membrane and protein trafficking through the endocytic and late secretory pathways. Its role as a molecular scaffold that drives formation of transport vesicles requires binding to a number of proteins with distinct functional and structural properties. Recent studies have revealed that most of these proteins interact with clathrin through surprisingly simple, linear arrangements of acidic and hydrophobic amino acid residues. This article discusses the different types of clathrin-binding proteins and motifs as well as the physiological significance of these proteins in clathrin-dependent events.
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Residues 212-216 of ARH comprise a clathrin box sequence (LLDLE) that mediates high affinity binding to the terminal domain of the heavy chain of clathrin.
“Residues 212-216 comprise a canonical clathrin box sequence (LLDLE) that mediates high affinity binding to the terminal domain of the heavy chain of clathrin (11,13,14).”
From The Modular Adaptor Protein Autosomal Recessive Hypercholesterolemia (ARH) Promotes Low Density Lipoprotein Receptor Clustering into Clathrin-coated Pits (2005) · cites this paper as [14]
The clathrin box consensus motif mediates binding of various proteins to the terminal domain of the clathrin heavy chain.
“that mediates binding of various proteins to the terminal domain of the clathrin heavy chain (18”
From ARH Is a Modular Adaptor Protein That Interacts with the LDL Receptor, Clathrin, and AP-2 (2002) · cites this paper as [18]
Four major regions of sequence conservation were identified in ARH: the N-terminal 44 amino acids, the PTB domain (residues 45 to 175), a 5-amino acid sequence similar to the clathrin box motif (LLDLE, residues 212-216), and a 27-amino acid sequence corresponding to residues 249-276 of human ARH.
“Four major regions of sequence conservation were identified: the N-terminal 44 amino acids, the PTB domain (residues 45 to 175), a 5-amino acid sequence similar to the clathrin box motif (LLDLE, residues 212–216) of other proteins (18”
From ARH Is a Modular Adaptor Protein That Interacts with the LDL Receptor, Clathrin, and AP-2 (2002) · cites this paper as [18]
Citations
Cites
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Cited by
Sorted by citations
Disabled‐2 exhibits the properties of a cargo‐selective endocytic clathrin adaptor
Mishra, S. K., Keyel, P. A., Hawryluk, M. J., Agostinelli, N. R., Watkins, S. C., & Traub, L. M. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf487 · Cited by 302
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
Garuti, R., Jones, C., Li, W.-P., Michaely, P., Herz, J., Gerard, R. D., Cohen, J. C., & Hobbs, H. H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509394200 · Cited by 91
Metadata
- Authors
- Dell'Angelica, E. C.
- Venue
- Trends in Cell Biology
- Publisher
- Elsevier BV
- Published
- 2001-08
- Volume
- 11
- Issue
- 8
- Pages
- 315-318
- ISSN
- 0962-8924
- Cited by
- 111
- References
- 2
- Language
- en
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