Evidence map›Paper›PMID 40845804›Full record

ArticleMolecular cell2025

The HIV-1 nuclear export complex reveals the role of RNA in CRM1 cargo recognition.

Amber M Smith, Yang Li, Arianna Velarde, Yifan Cheng, Alan D Frankel

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular cell, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Amber M SmithDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA.
Yang LiDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA.
Arianna VelardeDepartment of Biology, San Francisco State University, San Francisco, San Francisco, CA 94132, USA.
Yifan ChengDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA; Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, CA 94143, USA. Electronic address: yifan.cheng@ucsf.edu.
Alan D FrankelDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA. Electronic address: frankel@cgl.ucsf.edu.

Funding

X-ray Screening and Rapid Structure DeterminationP50GM082250 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KROGAN, NEVAN J · 2007 to 2018
$48.8M
Project 3U54AI170792 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ANDREJ SALI · 2022 to 2026
$35.7M
Acquisition of an electron microscope for high-resolution single particle cryo-EMS10OD021741 · OD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2016 to 2016
$2.0M
Glacios™ Cryo Transmission Electron Microscope with 200 kV XFEG opticsS10OD026881 · OD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2019 to 2019
$1.8M
Linux cluster for near atomic resolution single particle cryo-EMS10OD020054 · OD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2015 to 2015
$456k
GPU Computing Enabled Linux Computer ClusterS10RR026814 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2010 to 2010
$228k
NCRR NIH HHS S10 RR026814NIAID NIH HHS U54 AI170792NIGMS NIH HHS P50 GM082250NIH HHS S10 OD020054NIH HHS S10 OD021741NIH HHS S10 OD026881
6 · The paper itself

Abstract

HIV utilizes host proteins to manipulate cellular processes during replication. One key interaction involves the HIV regulatory protein Rev with the highly conserved nuclear exportin chromosome region maintenance 1(CRM1), which exports >1,000 proteins and ribonucleoprotein (RNP) complexes from the nucleus to the cytoplasm. Rev, with its associated viral RNA, is the first identified RNP cargo of CRM1. Here, we present the cryogenic-electron microscopy (cryo-EM) structure of the HIV-1 Rev/Rev response element (RRE)/CRM1/Ran nuclear export complex. A Rev dimer engages a unique CRM1 dimer at an uncharacterized cargo-binding site at the core of the complex, positioning the RRE within a charged pocket inside one CRM1 subunit. Direct contacts between the RNA and CRM1/Ran-guanosine triphosphate (GTP) highlight the critical role of the RRE. The structure, together with guided mutations and cellular assays, provides not only an unprecedented view of HIV RNA transport but also illuminates how CRM1 can recognize a diverse range of protein and RNP cargos.

Indexed as

HIV-1KaryopherinsReceptors, Cytoplasmic and Nuclearrev Gene Products, Human Immunodeficiency VirusRNA, ViralActive Transport, Cell NucleusBinding SitesCell NucleusCryoelectron MicroscopyExportin 1 ProteinGuanosine TriphosphateHumansModels, MolecularProtein BindingProtein Multimerizationran GTP-Binding ProteinExportin 1 ProteinGuanosine TriphosphateKaryopherinsran GTP-Binding ProteinRAN protein, humanReceptors, Cytoplasmic and Nuclearrev Gene Products, Human Immunodeficiency Virusrev protein, Human Immunodeficiency Virus-1RNA, ViralCRM1cryo-EMHIVnuclear exportRevribonucleoprotein complexesRNA

Identifiers

PMID40845804
PMCPMC12410093

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Registered trials

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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.