ArticleThe Journal of cell biology2000
HIV-1 rev depolymerizes microtubules to form stable bilayered rings.
Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 46 citations in OpenAlex.
- Structural basis of microtubule depolymerization by the kinesin-like activity of HIV-1 Rev.Structure (London, England : 1993) · 2023Article
- Self protein-protein interactions are involved in TPPP/p25 mediated microtubule bundling.Scientific reports · 2015Article
- Generation and use of antibody fragments for structural studies of proteins refractory to crystallization.Methods in molecular biology (Clifton, N.J.) · 2014Article
- Activity of the human immunodeficiency virus type 1 cell cycle-dependent internal ribosomal entry site is modulated by IRES trans-acting factors.Nucleic acids research · 2011Article
- Article
- Discovering regulated networks during HIV-1 latency and reactivation.Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing · 2006Article
- Early steps of retrovirus replicative cycle.Retrovirology · 2004Review
- Microtubule Dynamics may Embody a Stationary Bipolarity Forming Mechanism Related to the Prokaryotic Division Site Mechanism (Pole-to-Pole Oscillations).Journal of biological physics · 2004Article
Corrections and comments
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Authors and funding
7 authors at 5 institutions in 2 countries.
Funding
Abstract
We describe a novel interaction between HIV-1 Rev and microtubules (MTs) that results in the formation of bilayered rings that are 44-49 nm in external diameter, 3.4-4.2 MD (megadaltons) in mass, and have 28-, 30-, or 32-fold symmetry. Ring formation is not sensitive to taxol, colchicine, or microtubule-associated proteins, but requires Mg(2+) and is inhibited by maytansine. The interaction involves the NH(2)-terminal domain of Rev and the face of tubulin exposed on the exterior of the MTs. The NH(2)-terminal half of Rev has unexpected sequence similarity to the tubulin-binding portion of the catalytic/motor domains of the microtubule-destabilizing Kin I kinesins. We propose a model wherein binding of Rev dimers to MTs at their ends causes segments of two neighboring protofilaments to peel off and close into rings, circumferentially containing 14, 15, or 16 tubulin heterodimers, with Rev bound on the inside. Rev has a strong inhibitory effect on aster formation in Xenopus egg extracts, demonstrating that it can interact with tubulin in the presence of normal levels of cellular constituents. These results suggest that Rev may interact with MTs to induce their destabilization, a proposition consistent with the previously described disruption of MTs after HIV-1 infection.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.