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The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Simultaneous Binding of PtdIns(4,5)P 2 and Clathrin by AP180 in the Nucleation of Clathrin Lattices on Membranes

Ford, Marijn G. J., Pearse, Barbara M. F., Higgins, Matthew K., Vallis, Yvonne, Owen, David J., Gibson, Adele, Hopkins, Colin R., Evans, Philip R., McMahon, Harvey T.·2001·Science
DOI 10.1126/science.291.5506.1051
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Abstract

Adaptor protein 180 (AP180) and its homolog, clathrin assembly lymphoid myeloid leukemia protein (CALM), are closely related proteins that play important roles in clathrin-mediated endocytosis. Here, we present the structure of the NH 2 -terminal domain of CALM bound to phosphatidylinositol-4,5- bisphosphate [PtdIns(4,5)P 2 ] via a lysine-rich motif. This motif is found in other proteins predicted to have domains of similar structure (for example, Huntingtin interacting protein 1). The structure is in part similar to the epsin NH 2 -terminal (ENTH) domain, but epsin lacks the PtdIns(4,5)P 2 -binding site. Because AP180 could bind to PtdIns(4,5)P 2 and clathrin simultaneously, it may serve to tether clathrin to the membrane. This was shown by using purified components and a budding assay on preformed lipid monolayers. In the presence of AP180, clathrin lattices formed on the monolayer. When AP2 was also present, coated pits were formed.

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Crossref · 10.1126/science.291.5506.1051

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1 of 1 references verified0 citation errors · 0 not checkable

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  • Oriented on a 10% PtdIns(4,5)P2-containing monolayer, GST-Dab2(1-368) recruits soluble clathrin and drives the formation of regular polyhedral structures.

    “Oriented in this way upon a 10% PtdIns(4,5)P 2 -containing monolayer of mixed lipids (Ford et al., 2001), the protein is able to recruit soluble clathrin and drive the formation of regular polyhedral structures (Figure 8A and B), which, alone, does not associate with the monolayer (Figure 8A, inset, see C, lane b).”

    From Disabled‐2 exhibits the properties of a cargo‐selective endocytic clathrin adaptor (2002) · cites this paper as Ford et al., 2001

  • Approximately one-quarter of the liposome-bound coat components are resistant to extraction with 1% Triton X-100.

    “Approximately one-quarter of the liposome-bound coat components are resistant to extraction with 1% Triton X-100 (Figure 8C, lane j), which has been shown by others to correlate well with extensive assembly into curved polyhedral coats (Ford et al., 2001).”

    From Disabled‐2 exhibits the properties of a cargo‐selective endocytic clathrin adaptor (2002) · cites this paper as Ford et al., 2001

  • Extensive clathrin recruitment does not disrupt the interaction between AP-2 and either Dab2 or epsin, AP180 or HIP1.

    “Importantly, and in contrast to eps15 (Cupers et al., 1998), extensive clathrin recruitment does not disrupt the interaction between AP-2 and either Dab2 or epsin (Figure 8) (Mishra et al., 2001), AP180 (Ford et al., 2001) or HIP1 (Mishra et al., 2001), such that these proteins are now released from the membrane surface.”

    From Disabled‐2 exhibits the properties of a cargo‐selective endocytic clathrin adaptor (2002) · cites this paper as Ford et al., 2001

  • The PtdIns(4,5)P2-, AP-2- and clathrin-binding properties facilitate Dab2 placement at the bud site.

    “The PtdIns(4,5)P 2 -, AP-2-and clathrin-binding properties will facilitate Dab2 placement at the bud site, as do analogous determinants in AP180, epsin and HIP1 (Ford et al., 2001;Mishra et al., 2001).”

    From Disabled‐2 exhibits the properties of a cargo‐selective endocytic clathrin adaptor (2002) · cites this paper as Ford et al., 2001

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Metadata

Authors
Ford, M. G. J., Pearse, B. M. F., Higgins, M. K., Vallis, Y., Owen, D. J., Gibson, A., Hopkins, C. R., Evans, P. R., & McMahon, H. T.
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
2001-02-09
Volume
291
Issue
5506
Pages
1051-1055
ISSN
  • 0036-8075
  • 1095-9203
DOI
10.1126/science.291.5506.1051
Cited by
659
References
1
Language
en

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