(Q46069109)

19 December 2017

title

New function of the proline rich domain in dynamin-2 to negatively regulate its interaction with microtubules in mammalian cells (English)

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19 December 2017

author name string

Kozue Hamao

series ordinal

1

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19 December 2017

Makiko Morita

series ordinal

2

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19 December 2017

Hiroshi Hosoya

series ordinal

3

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19 December 2017

language of work or name

English

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publication date

10 February 2009

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19 December 2017

Experimental Cell Research

published in

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19 December 2017

volume

315

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19 December 2017

issue

7

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19 December 2017

page(s)

1336-1345

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19 December 2017

Microtubule-organizing centers and cell migration: effect of inhibition of migration and microtubule disruption in endothelial cells

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Dynamin is a GTPase stimulated to high levels of activity by microtubules

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Microtubules and Src homology 3 domains stimulate the dynamin GTPase via its C-terminal domain

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The large GTPase dynamin associates with the spindle midzone and is required for cytokinesis

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Differential distribution of dynamin isoforms in mammalian cells

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Role of the proline-rich domain of dynamin-2 and its interactions with Src homology 3 domains during endocytosis of the AT1 angiotensin receptor

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Rho-kinase contributes to diphosphorylation of myosin II regulatory light chain in nonmuscle cells

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GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission

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Real-time detection reveals that effectors couple dynamin's GTP-dependent conformational changes to the membrane.

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Microtubule-associated protein MAP2 shares a microtubule binding motif with tau protein.

7 January 2021

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Functional interactions between the proline-rich and repeat regions of tau enhance microtubule binding and assembly

7 January 2021

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A microtubule-binding domain in dynactin increases dynein processivity by skating along microtubules.

7 January 2021

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7 January 2021

Identifiers

DOI

1 reference

19 December 2017

PubMed ID

19331814

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19 December 2017