Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling (Q27648705)

GOA release 2020-03-11

1

Oliver Daumke

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author name string

Richard Lundmark

2

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Yvonne Vallis

3

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Sascha Martens

4

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P Jonathan G Butler

5

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Harvey T McMahon

The dynamin superfamily: universal membrane tubulation and fission molecules?

6

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language of work or name

English

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publication date

18 October 2007

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published in

Nature

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volume

449

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page(s)

923-7

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issue

7164

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cites work

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EHD proteins are associated with tubular and vesicular compartments and interact with specific phospholipids.

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Association of insulin-like growth factor 1 receptor with EHD1 and SNAP29

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Pincher-mediated macroendocytosis underlies retrograde signaling by neurotrophin receptors.

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EHD proteins associate with syndapin I and II and such interactions play a crucial role in endosomal recycling.

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ATP binding regulates oligomerization and endosome association of RME-1 family proteins

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EHD2 and the novel EH domain binding protein EHBP1 couple endocytosis to the actin cytoskeleton

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How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP

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Molecular mechanism of NPF recognition by EH domains

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GTPase activity of dynamin and resulting conformation change are essential for endocytosis

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Identifiers

DOI

10.1038/NATURE06173

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Consolidated OpenCitations Corpus – April 2017

Dimensions Publication ID

1017889

1005633966

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1017889

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Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference