ArticleMolecular and cellular biology2005
Kinetic and molecular analysis of nuclear export factor CRM1 association with its cargo in vivo.
Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
40 citing papers in PubMed, 66 citations in OpenAlex.
- Structure of HIV-1 RRE stem-loop II identifies two conformational states of the high-affinity Rev binding site.Nature communications · 2024Article
- Mechanism of exportin retention in the cell nucleus.The Journal of cell biology · 2024Article
- SET-CAN/NUP214 fusion gene in leukemia: general features and clinical advances.Frontiers in oncology · 2023Review
- STRUCTURED CORRELATION DETECTION WITH APPLICATION TO COLOCALIZATION ANALYSIS IN DUAL-CHANNEL FLUORESCENCE MICROSCOPIC IMAGING.Statistica Sinica · 2021Article
- Cotargeting of XPO1 Enhances the Antileukemic Activity of Midostaurin and Gilteritinib in Acute Myeloid Leukemia.Cancers · 2020Article
- Review
- Sequence and Functional Variation in the HIV-1 Rev Regulatory Axis.Current HIV research · 2020Article
- Nucleolar Localization of HIV-1 Rev Is Required, Yet Insufficient for Production of Infectious Viral Particles.AIDS research and human retroviruses · 2018Article
- The Interplay of Viral and Host Factors in Chikungunya Virus Infection: Targets for Antiviral Strategies.Viruses · 2018Review
- Is unphosphorylated Rex, as multifunctional protein of HTLV-1, a fully intrinsically disordered protein? An in silico study.Biochemistry and biophysics reports · 2016Article
- Leukemia-Associated Nup214 Fusion Proteins Disturb the XPO1-Mediated Nuclear-Cytoplasmic Transport Pathway and Thereby the NF-κB Signaling Pathway.Molecular and cellular biology · 2016Article
- CRM1 inhibitor S109 suppresses cell proliferation and induces cell cycle arrest in renal cancer cells.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2016Article
- Human Exportin-1 is a Target for Combined Therapy of HIV and AIDS Related Lymphoma.EBioMedicine · 2015Article
- Mining the human complexome database identifies RBM14 as an XPO1-associated protein involved in HIV-1 Rev function.Journal of virology · 2015Article
- A HIV-1 Tat mutant protein disrupts HIV-1 Rev function by targeting the DEAD-box RNA helicase DDX1.Retrovirology · 2014Article
- Cooperativity among Rev-associated nuclear export signals regulates HIV-1 gene expression and is a determinant of virus species tropism.Journal of virology · 2014Article
- Biologic activity of the novel orally bioavailable selective inhibitor of nuclear export (SINE) KPT-335 against canine melanoma cell lines.BMC veterinary research · 2014Article
- Stable assembly of HIV-1 export complexes occurs cotranscriptionally.RNA (New York, N.Y.) · 2014Article
- Article
- Mapping the binding interface between an HIV-1 inhibiting intrabody and the viral protein Rev.PloS one · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The nucleocytoplasmic transport receptor CRM1 mediates the export of macromolecules from the nucleus to the cytoplasm by forming a ternary complex with a cargo molecule and RanGTP. The in vivo mechanism of CRM1 export complex formation and its mobility throughout the nucleus have not been fully elucidated. More information is required to fully understand complex formation and the dynamics of CRM1-cargo-RanGTP complexes in space and time. We demonstrate true molecular interaction of CRM1 with its Rev cargo in living cells by using fluorescence resonance energy transfer (FRET). Interestingly, we found that the inhibitory effect of leptomycin B on this CRM1-cargo interaction is Ran dependent. Using fluorescence recovery after photobleaching (FRAP), we show that CRM1 moves at rates similar to that of free green fluorescent protein in the nucleoplasm. A slower mobility was detected on the nuclear membrane, consistent with known CRM1 interactions with nuclear pores. Based on these data, we propose an in vivo model in which CRM1 roams through the nucleus in search of high-affinity binding sites. CRM1 is able to bind Rev cargo in the nucleolus, and upon RanGTP binding a functional export complex is produced that is exported to the cytoplasm.
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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.