Curvature of clathrin-coated pits driven by epsin (Q27639716)

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Ian G Mills

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Brian J Peter

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Yvonne Vallis

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Gerrit J K Praefcke

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Philip R Evans

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Harvey T McMahon

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language of work or name

English

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publication date

26 September 2002

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published in

Nature

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volume

419

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issue

6905

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page(s)

361-6

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cites work

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Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis

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Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis

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

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Epsin 1 undergoes nucleocytosolic shuttling and its eps15 interactor NH(2)-terminal homology (ENTH) domain, structurally similar to Armadillo and HEAT repeats, interacts with the transcription factor promyelocytic leukemia Zn(2)+ finger protein (PLZ

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Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis

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Unusual structural organization of the endocytic proteins AP180 and epsin 1

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Amphiphysin is necessary for organization of the excitation-contraction coupling machinery of muscles, but not for synaptic vesicle endocytosis in Drosophila

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Endophilin I mediates synaptic vesicle formation by transfer of arachidonate to lysophosphatidic acid.

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Epsin binds to clathrin by associating directly with the clathrin-terminal domain. Evidence for cooperative binding through two discrete sites.

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Dynamin undergoes a GTP-dependent conformational change causing vesiculation

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Synaptic vesicle size and number are regulated by a clathrin adaptor protein required for endocytosis

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Eps15 is a component of clathrin-coated pits and vesicles and is located at the rim of coated pits

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