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Disabled‐2 Colocalizes with the LDLR in Clathrin‐Coated Pits and Interacts with AP‐2

Morris, Shelli M., Cooper, Jonathan A.·2001·Traffic
DOI 10.1034/j.1600-0854.2001.020206.x
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Abstract

Disabled‐2 (Dab2) is a widely expressed relative of Disabled‐1, a neuron‐specific signal‐transduction protein that binds to and receives signals from members of the low‐density lipoprotein receptor (LDLR) family. Members of the LDLR family internalize through clathrin‐coated pits and vesicles to endosomes, from where they return to the cell surface through the secretory pathway. In this study, we show that the Dab2 phosphotyrosine‐binding domain binds peptides containing the sequence FXNPXY. This core sequence is found in the intracellular domains of LDLR family members and is important for receptor internalization. Dab2 transiently colocalizes with the LDLR in clathrin‐coated pits, but is absent from endosomes and lysosomes. Dab2 is alternatively spliced and its localization depends on a region of the protein that contains two DPF motifs that are present in the p96 Dab2 protein and absent in the p67 splice variant. This region is sufficient to confer Dab2 binding to the α‐adaptin subunit of the clathrin adaptor protein, AP‐2. Overexpression of p96 but not of p67 Dab2 disrupts the localization of AP‐2. These findings suggest that in addition to previously reported signal‐transduction functions, Dab2 could also act as an adaptor protein that may regulate protein trafficking.

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  • Pre-incubating liposomes with a mixture of AP-2 and GST-Dab2 increases the recovery of both proteins in the liposome pellet.

    “Pre-incubating liposomes together with a mixture of AP-2 and the GST±Dab2 fusion increases the recovery of both proteins in the liposome pellet (Figure 8C, lane h), validating the AP-2±Dab2 interactions seen in pull-down assays (Figures 1 and 2) (Morris and Cooper, 2001).”

    From Disabled‐2 exhibits the properties of a cargo‐selective endocytic clathrin adaptor (2002) · cites this paper as Morris and Cooper, 2001

  • Dab2 binds AP-2 directly via a central portion that engages the AP-2 alpha-subunit appendage.

    “Dab2 binds to AP-2 directly via a central portion that, like epsin, AP180 and HIP1, engages the independently folded appendage domain of the AP-2 a-subunit (Morris and Cooper, 2001).”

    From Disabled‐2 exhibits the properties of a cargo‐selective endocytic clathrin adaptor (2002) · cites this paper as Morris and Cooper, 2001

  • In cultured cells, Dab2 plays a role in the endocytosis of LDL receptor, in coordination with Arh.

    “In studies using cultured cells, Dab2 was found to play a role in the endocytosis of LDL receptor, in coordination with Arh”

    From Endocytosis and Physiology: Insights from Disabled-2 Deficient Mice (2016) · cites this paper as Morris and Cooper, 2001

  • Exogenously expressed mCherry-labeled Dab2 colocalizes with clathrin-coat components in control cells.

    “In agreement with previous studies (Morris and Cooper, 2001; Keyel et al., 2006; Maurer and Cooper, 2006; Chetrit et al., 2009), we observed colocalization of exogenously expressed mCherry-labeled Dab2 with clathrin-coat components in control cells.”

    From Cargo- and adaptor-specific mechanisms regulate clathrin-mediated endocytosis (2010) · cites this paper as Morris and Cooper, 2001

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Metadata

Authors
Morris, S. M., & Cooper, J. A.
Venue
Traffic
Publisher
Wiley
Published
2001-01
Volume
2
Issue
2
Pages
111-123
ISSN
  • 1398-9219
  • 1600-0854
DOI
10.1034/j.1600-0854.2001.020206.x
Cited by
222
References
2
Language
en
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor, 354 d)

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