MxA, a member of the dynamin superfamily, interacts with the ankyrin-like repeat domain of TRPC (Q24297807)

1

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Sylvie Cayouette

2

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Pascale K Lepage

3

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Cynthia L Bernier

4

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Nancy Francoeur

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Marie St-Hilaire

6

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Maxime Pinard

7

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Guylain Boulay

Journal of Biological Chemistry

8

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language of work or name

English

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publication date

13 May 2005

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published in

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volume

280

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issue

19

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page(s)

19393-400

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cites work

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Inhibitor of Myogenic Family, a Novel Suppressor of Store-operated Currents through an Interaction with TRPC1

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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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The calcineurin-binding protein cain is a negative regulator of synaptic vesicle endocytosis

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The antiviral dynamin family member, MxA, tubulates lipids and localizes to the smooth endoplasmic reticulum

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Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding

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Dynamin undergoes a GTP-dependent conformational change causing vesiculation.

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

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Antivirally active MxA protein sequesters La Crosse virus nucleocapsid protein into perinuclear complexes

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Missorting of LaCrosse virus nucleocapsid protein by the interferon-induced MxA GTPase involves smooth ER membranes

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A monomeric GTPase-negative MxA mutant with antiviral activity

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Interferon-induced antiviral Mx1 GTPase is associated with components of the SUMO-1 system and promyelocytic leukemia protein nuclear bodies

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Protein modification by SUMO

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Calcium - a life and death signal

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Nucleotide-dependent conformational changes in dynamin: evidence for a mechanochemical molecular spring

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