Fission and uncoating of synaptic clathrin-coated vesicles are perturbed by disruption of interactions with the SH3 domain of endophilin. (Q30168754)

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10 November 2019

title

Fission and uncoating of synaptic clathrin-coated vesicles are perturbed by disruption of interactions with the SH3 domain of endophilin (English)

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10 November 2019

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1

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10 November 2019

Oleg Shupliakov

12

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10 November 2019

author name string

N Ringstad

2

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10 November 2019

P Löw

3

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10 November 2019

O Kjaerulff

4

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10 November 2019

J Gustafsson

5

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10 November 2019

M Wenk

6

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10 November 2019

G Di Paolo

7

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10 November 2019

Y Nemoto

8

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10 November 2019

J Crun

9

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10 November 2019

M H Ellisman

10

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10 November 2019

P De Camilli

11

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10 November 2019

L Brodin

13

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10 November 2019

publication date

1 August 2000

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10 November 2019

language of work or name

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10 November 2019

volume

27

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10 November 2019

issue

2

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10 November 2019

page(s)

301-312

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Coupled inositide phosphorylation and phospholipase D activation initiates clathrin-coat assembly on lysosomes.

10 November 2019

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The SH3 domains of endophilin and amphiphysin bind to the proline-rich region of synaptojanin 1 at distinct sites that display an unconventional binding specificity

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SAC1-like domains of yeast SAC1, INP52, and INP53 and of human synaptojanin encode polyphosphoinositide phosphatases

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Regulation of AP-3 function by inositides. Identification of phosphatidylinositol 3,4,5-trisphosphate as a potent ligand

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7 January 2021

Synaptic vesicles retain their identity through the endocytic cycle

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Crystal structure of the amphiphysin-2 SH3 domain and its role in the prevention of dynamin ring formation

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Identifiers

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10 November 2019

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