The N terminus of amphiphysin II mediates dimerization and plasma membrane targeting (Q28138629)

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J Philie

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E de Heuvel

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P S McPherson

Journal of Biological Chemistry

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language of work or name

English

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publication date

9 July 1999

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published in

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volume

274

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issue

28

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page(s)

19785-91

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cites work

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A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals

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A new member of the amphiphysin family connecting endocytosis and signal transduction pathways

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The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding consensus sequence

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Synaptojanin forms two separate complexes in the nerve terminal. Interactions with endophilin and amphiphysin

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Role of phosphorylation in regulation of the assembly of endocytic coat complexes

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Inhibition of receptor-mediated endocytosis by the amphiphysin SH3 domain

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Synaptic vesicle endocytosis impaired by disruption of dynamin-SH3 domain interactions

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Clathrin interacts specifically with amphiphysin and is displaced by dynamin1

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Multiple amphiphysin II splice variants display differential clathrin binding: identification of two distinct clathrin-binding sites

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Structural analysis of the human BIN1 gene. Evidence for tissue-specific transcriptional regulation and alternate RNA splicing

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The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15.

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SH3 domain‐dependent interactions of endophilin with amphiphysin

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