Phosphorylation of APOBEC3G by protein kinase A regulates its interaction with HIV-1 Vif. (Q39932323)

15 September 2017

Phosphorylation of APOBEC3G by protein kinase A regulates its interaction with HIV-1 Vif. (English)

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15 September 2017

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Takashi Uchiyama

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15 September 2017

Kotaro Shirakawa

1

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15 September 2017

Akifumi Takaori-Kondo

2

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15 September 2017

Masaru Yokoyama

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15 September 2017

Taisuke Izumi

4

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15 September 2017

Masashi Matsui

5

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15 September 2017

Katsuhiro Io

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15 September 2017

Toshihiro Sato

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15 September 2017

Hironori Sato

8

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15 September 2017

5 October 2008

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Nature Structural & Molecular Biology

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1184-1191

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https://scigraph.springernature.com/pub.10.1038/nsmb.1497

15 September 2017

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The enzymatic activity of CEM15/Apobec-3G is essential for the regulation of the infectivity of HIV-1 virion but not a sole determinant of its antiviral activity.

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Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function

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The AID antibody diversification enzyme is regulated by protein kinase A phosphorylation

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Active cAMP-dependent protein kinase incorporated within highly purified HIV-1 particles is required for viral infectivity and interacts with viral capsid protein

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Human immunodeficiency virus proteins induce the inhibitory cAMP/protein kinase A pathway in normal lymphocytes

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A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion

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A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action

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A single amino acid difference in the host APOBEC3G protein controls the primate species specificity of HIV type 1 virion infectivity factor

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A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif).

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APOBEC3G targets specific virus species.

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The HIV 'A' (sor) gene product is essential for virus infectivity

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31 March 2020

Identifiers

DOI

10.1038/NSMB.1497

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Dimensions Publication ID

15 September 2017

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