The Pleckstrin Homology Domains of Dynamin Isoforms Require Oligomerization for High Affinity Phosphoinositide Binding (Q54246386)

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5 December 2019

title

The pleckstrin homology domains of dynamin isoforms require oligomerization for high affinity phosphoinositide binding (English)

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5 December 2019

4

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5 December 2019

Mark A. Lemmon

5

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5 December 2019

author name string

D E Klein

1

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5 December 2019

A Lee

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5 December 2019

D W Frank

3

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5 December 2019

language of work or name

English

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publication date

1 October 1998

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Journal of Biological Chemistry

5 December 2019

published in

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5 December 2019

volume

273

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5 December 2019

page(s)

27725-27733

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5 December 2019

issue

42

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Dynamin GTPase, a force-generating molecular switch.

5 December 2019

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A binding site for SH3 domains targets dynamin to coated pits

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Synergistic activation of dynamin GTPase by Grb2 and phosphoinositides

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Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain

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Crystal structure at 2.2 A resolution of the pleckstrin homology domain from human dynamin

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Identification of the Binding Site for Acidic Phospholipids on the PH Domain of Dynamin: Implications for Stimulation of GTPase Activity

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Specific role for the PH domain of dynamin-1 in the regulation of rapid endocytosis in adrenal chromaffin cells

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