Science. 2001 Feb 9;291(5506):1051-5.

Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes.

Ford MG, Pearse BM, Higgins MK, Vallis Y, Owen DJ, Gibson A, Hopkins CR, Evans PR, McMahon HT.

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Medical Research Council (MRC) Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK.

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 NH2-terminal domain of CALM bound to phosphatidylinositol-4,5- bisphosphate [PtdIns(4,5)P2] 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 NH2-terminal (ENTH) domain, but epsin lacks the PtdIns(4,5)P2-binding site. Because AP180 could bind to PtdIns(4,5)P2 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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Cell biology. A lipid oils the endocytosis machine. [Science. 2001]
Cell biology. A lipid oils the endocytosis machine.Gillooly DJ, Stenmark H. Science. 2001 Feb 9; 291(5506):993-4.

PMID:: 11161218; [PubMed - indexed for MEDLINE]

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Structures reported by this article

Calm-N N-Terminal Domain Of Clathrin Assembly Lymphoid Myeloid Leukaemia Protein, Inositol(4,5)p2 Complex

PDB: 1HG2

Source: Rattus norvegicus

Method: X-Ray Diffraction

Resolution: 2 Å

See all 4 structures...

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Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the nucleation of...
Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes.
Science. 2001 Feb 9 ;291(5506):1051-5.

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