ArticleThe Journal of biological chemistry2011
A minimal nuclear localization signal (NLS) in human phospholipid scramblase 4 that binds only the minor NLS-binding site of importin alpha1.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 60 citations in OpenAlex.
- Structures of Nicotiana benthamiana importin-α1 complexes reveal mechanisms for plant virus NLS recognition.The Plant journal : for cell and molecular biology · 2026Article
- Highly efficient expression of DNA-peptide conjugates in growth-arrested cells.Nature communications · 2026Article
- Nucleolar beacon for monitoring nucleolar morphology and proteomics in living cells.Science advances · 2025Article
- Review
- Henipavirus Matrix Protein Employs a Non-Classical Nuclear Localization Signal Binding Mechanism.Viruses · 2023Article
- Article
- Karyopherin-mediated nucleocytoplasmic transport.Nature reviews. Molecular cell biology · 2022Review
- Identification and characterisation of a phospholipid scramblase in the malaria parasite Plasmodium falciparum.Molecular and biochemical parasitology · 2021Article
- Article
- Review
- The Shigella type three secretion system effector OspF invades host nucleus by binding host importin α1.World journal of microbiology & biotechnology · 2019Article
- Correlation of CRM1-NES affinity with nuclear export activity.Molecular biology of the cell · 2018Article
- Variations in nuclear localization strategies among pol X family enzymes.Traffic (Copenhagen, Denmark) · 2018Article
- STAT3 Cooperates With Phospholipid Scramblase 2 to Suppress Type I Interferon Response.Frontiers in immunology · 2018Article
- Three-dimensional context rather than NLS amino acid sequence determines importin α subtype specificity for RCC1.Nature communications · 2017Article
- Synergy of two low-affinity NLSs determines the high avidity of influenza A virus nucleoprotein NP for human importin α isoforms.Scientific reports · 2017Article
- Divergent Evolution of Nuclear Localization Signal Sequences in Herpesvirus Terminase Subunits.The Journal of biological chemistry · 2016Article
- PARP-2 domain requirements for DNA damage-dependent activation and localization to sites of DNA damage.Nucleic acids research · 2016Article
- Molecular Components of the Neurospora crassa pH Signaling Pathway and Their Regulation by pH and the PAC-3 Transcription Factor.PloS one · 2016Article
- Tubby-like protein superfamily member PLSCR3 functions as a negative regulator of adipogenesis in mouse 3T3-L1 preadipocytes by suppressing induction of late differentiation stage transcription factors.Bioscience reports · 2015Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Importin α1 can bind classical nuclear localization signals (NLSs) in two NLS-binding sites, known as "major" and "minor." The major site is located between ARM repeats 2-4, whereas the minor site spans ARM 7-8. In this study, we have characterized the cellular localization of human phospholipid scramblase 4 (hPLSCR4), a member of the phospholipid scramblase protein family. We identified a minimal NLS in hPLSCR4 ((273)GSIIRKWN(280)) that contains only two basic amino acids. This NLS is both necessary for nuclear localization of hPLSCR4 in transfected HeLa cells and sufficient for nuclear import of a non-diffusible cargo in permeabilized cells. Mutation of only one of the two basic residues, Arg(277), correlates with loss of nuclear localization, suggesting this amino acid plays a key role in nuclear transport. Crystallographic analysis of mammalian importin α1 in complex with the hPLSCR4-NLS reveals this minimal NLS binds specifically and exclusively to the minor binding site of importin α. These data provide the first structural and functional evidence of a novel NLS-binding mode in importin α1 that uses only the minor groove as the exclusive site for nuclear import of nonclassical cargos.
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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.