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- W4385769618 endingPage "1246.e5" @default.
- W4385769618 startingPage "1233" @default.
- W4385769618 abstract "HIV-1 Rev is an essential regulatory protein that transports unspliced and partially spliced viral mRNAs from the nucleus to the cytoplasm for the expression of viral structural proteins. During its nucleocytoplasmic shuttling, Rev interacts with several host proteins to use the cellular machinery for the advantage of the virus. Here, we report the 3.5 Å cryo-EM structure of a 4.8 MDa Rev-tubulin ring complex. Our structure shows that Rev's arginine-rich motif (ARM) binds to both the acidic surfaces and the C-terminal tails of α/β-tubulin. The Rev-tubulin interaction is functionally homologous to that of kinesin-13, potently destabilizing microtubules at sub-stoichiometric levels. Expression of Rev in astrocytes and HeLa cells shows that it can modulate the microtubule cytoskeleton within the cellular environment. These results show a previously undefined regulatory role of Rev." @default.
- W4385769618 created "2023-08-12" @default.
- W4385769618 creator A5019575606 @default.
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- W4385769618 creator A5065079947 @default.
- W4385769618 creator A5081244046 @default.
- W4385769618 creator A5090836640 @default.
- W4385769618 date "2023-10-01" @default.
- W4385769618 modified "2023-10-12" @default.
- W4385769618 title "Structural basis of microtubule depolymerization by the kinesin-like activity of HIV-1 Rev" @default.
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