ReviewThe FEBS journal2014
Allosteric control of the exportin CRM1 unraveled by crystal structure analysis.
Review in The FEBS journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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.
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.
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Who cites it
20 citing papers in PubMed, 39 citations in OpenAlex.
- A USP28-TM9SF3-Golgiphagy axis maintains glycosylation homeostasis and promotes breast cancer progression.The EMBO journal · 2026Article
- A multivalent adaptor mechanism drives the nuclear import of proteasomes.Nature communications · 2026Article
- The HIV-1 nuclear export complex reveals the role of RNA in CRM1 cargo recognition.Molecular cell · 2025Article
- Structural basis for a nucleoporin exportin complex between RanBP2, SUMO1-RanGAP1, the E2 Ubc9, Crm1 and the Ran GTPase.Nature communications · 2025Article
- A CRM1-dependent nuclear export signal inJournal of virology · 2024Article
- CD47 interactions with exportin-1 limit the targeting of mJournal of cell communication and signaling · 2022Article
- RanGTPase links nucleo-cytoplasmic transport to the recruitment of cargoes into small extracellular vesicles.Cellular and molecular life sciences : CMLS · 2022Article
- OsWRKY62 and OsWRKY76 Interact with Importin α1s for Negative Regulation of Defensive Responses in Rice Nucleus.Rice (New York, N.Y.) · 2022Article
- XPO1-Mediated EIF1AX Cytoplasmic Relocation Promotes Tumor Migration and Invasion in Endometrial Carcinoma.Oxidative medicine and cellular longevity · 2022Article
- AMPK Localization: A Key to Differential Energy Regulation.International journal of molecular sciences · 2021Review
- The nuclear export protein XPO1 - from biology to targeted therapy.Nature reviews. Clinical oncology · 2021Review
- Article
- Establishment of the early cilia preassembly protein complex during motile ciliogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Leptomycin B alters the subcellular distribution of CRM1 (Exportin 1).Biochemical and biophysical research communications · 2017Article
- A cellular reporter to evaluate CRM1 nuclear export activity: functional analysis of the cancer-related mutant E571K.Cellular and molecular life sciences : CMLS · 2016Article
- The RanBP2/RanGAP1*SUMO1/Ubc9 SUMO E3 ligase is a disassembly machine for Crm1-dependent nuclear export complexes.Nature communications · 2016Article
- Oncogenic role of p21 in hepatocarcinogenesis suggests a new treatment strategy.World journal of gastroenterology · 2015Review
- Review
- Small GTP-binding protein Ran is regulated by posttranslational lysine acetylation.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Introduction: celebrating the international year of crystallography: introduction.The FEBS journal · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nucleocytoplasmic trafficking in eukaryotic cells is a highly regulated and coordinated process which involves an increasing variety of soluble nuclear transport receptors. Generally, transport receptors specifically bind their cargo and facilitate its transition through nuclear pore complexes, aqueous channels connecting the two compartments. Directionality of such transport events by receptors of the importin β superfamily requires the interaction with the small GTPase Ras-related nuclear antigen (Ran). While importins need RanGTP to release their cargo in the nucleus and thus to terminate import, exportins recruit cargo in the RanGTP-bound state. The exportin chromosome region maintenance 1 (CRM1) is a highly versatile transport receptor that exports a plethora of different protein and RNP cargoes. Moreover, binding of RanGTP and of cargo to CRM1 are highly cooperative events despite the fact that cargo and RanGTP do not interact directly in crystal structures of assembled export complexes. Integrative approaches have recently unraveled the individual steps of the CRM1 transport cycle at a structural level and explained how the HEAT-repeat architecture of CRM1 provides a framework for the key elements to mediate allosteric interactions with RanGTP, Ran binding proteins and cargo. Moreover, during the last decade, CRM1 has become a more and more appreciated target for anti-cancer drugs. Hence, detailed understanding of the flexibility, the regulatory features and the positive binding cooperativity between CRM1, Ran and cargo is a prerequisite for the development of highly effective drugs. Here we review recent structural advances in the characterization of CRM1 and CRM1-containing complexes with a special emphasis on X-ray crystallographic studies.
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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.