ArticleMolecular and cellular biology1998
Identification and functional characterization of a novel nuclear localization signal present in the yeast Nab2 poly(A)+ RNA binding protein.
Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 64 citations in OpenAlex.
- A kinetic ruler controls mRNA poly(A) tail length.Genes & development · 2025Article
- Characterization of HNRNPA1 mutations defines diversity in pathogenic mechanisms and clinical presentation.JCI insight · 2021Article
- Age-dependent deterioration of nuclear pore assembly in mitotic cells decreases transport dynamics.eLife · 2019Article
- The multitasking polyA tail: nuclear RNA maturation, degradation and export.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Rhinovirus 3C protease facilitates specific nucleoporin cleavage and mislocalisation of nuclear proteins in infected host cells.PloS one · 2013Article
- The long and the short of it: the role of the zinc finger polyadenosine RNA binding protein, Nab2, in control of poly(A) tail length.Biochimica et biophysica acta · 2012Review
- Nuclear import by karyopherin-βs: recognition and inhibition.Biochimica et biophysica acta · 2011Review
- Article
- Expanding the definition of the classical bipartite nuclear localization signal.Traffic (Copenhagen, Denmark) · 2010Article
- Purification of nuclear poly(A)-binding protein Nab2 reveals association with the yeast transcriptome and a messenger ribonucleoprotein core structure.The Journal of biological chemistry · 2009Article
- Transportin regulates major mitotic assembly events: from spindle to nuclear pore assembly.Molecular biology of the cell · 2009Article
- Kap104p imports the PY-NLS-containing transcription factor Tfg2p into the nucleus.The Journal of biological chemistry · 2009Article
- Modular organization and combinatorial energetics of proline-tyrosine nuclear localization signals.PLoS biology · 2008Article
- A PY-NLS nuclear targeting signal is required for nuclear localization and function of the Saccharomyces cerevisiae mRNA-binding protein Hrp1.The Journal of biological chemistry · 2008Article
- Structure of the N-terminal Mlp1-binding domain of the Saccharomyces cerevisiae mRNA-binding protein, Nab2.Journal of molecular biology · 2008Article
- Arabidopsis transportin1 is the nuclear import receptor for the circadian clock-regulated RNA-binding protein AtGRP7.Plant molecular biology · 2003Article
- Nuclear import of zinc binuclear cluster proteins proceeds through multiple, overlapping transport pathways.Eukaryotic cell · 2003Article
- Effect of the pheromone-responsive G(alpha) and phosphatase proteins of Saccharomyces cerevisiae on the subcellular localization of the Fus3 mitogen-activated protein kinase.Molecular and cellular biology · 2003Article
- Methylation of Xenopus CIRP2 regulates its arginine- and glycine-rich region-mediated nucleocytoplasmic distribution.Nucleic acids research · 2002Article
- Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nuclear import of proteins bearing a basic nuclear localization signal (NLS) is dependent on karyopherin alpha/importin alpha, which acts as the NLS receptor, and karyopherin beta1/importin beta, which binds karyopherin alpha and mediates the nuclear import of the resultant ternary complex. Recently, a second nuclear import pathway that allows the rapid reentry into the nucleus of proteins that participate in the nuclear export of mature mRNAs has been identified. In mammalian cells, a single NLS specific for this alternate pathway, the M9 NLS of heterogeneous nuclear ribonucleoprotein A1 (hnRNPA1), has been described. The M9 NLS binds a transport factor related to karyopherin beta1, termed karyopherin beta2 or transportin, and does not require a karyopherin alpha-like adapter protein. A yeast homolog of karyopherin beta2, termed Kap104p, has also been described and proposed to play a role in the nuclear import of a yeast hnRNP-like protein termed Nab2p. Here, we define a Nab2p sequence that binds to Kap104p and that functions as an NLS in both human and yeast cells despite lacking any evident similarity to basic or M9 NLSs. Using an in vitro nuclear import assay, we demonstrate that Kap104p can direct the import into isolated human cell nuclei of a substrate containing a wild-type, but not a defective mutant, Nab2p NLS. In contrast, other NLSs, including the M9 NLS, could not function as substrates for Kap104p. Surprisingly, this in vitro assay also revealed that human karyopherin beta1, but not the Kap104p homolog karyopherin beta2, could direct the efficient nuclear import of a Nab2p NLS substrate in vitro in the absence of karyopherin alpha. These data therefore identify a novel NLS sequence, active in both yeast and mammalian cells, that is functionally distinct from both basic and M9 NLS sequences.
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