ArticleProceedings of the National Academy of Sciences of the United States of America1995
Isolation of a yeast protein kinase that is activated by the protein encoded by SRP1 (Srp1p) and phosphorylates Srp1p complexed with nuclear localization signal peptides.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 28 citations in OpenAlex.
- Regulation of protein kinase Cδ Nuclear Import and Apoptosis by Mechanistic Target of Rapamycin Complex-1.Scientific reports · 2019Article
- Importin α: functions as a nuclear transport factor and beyond.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2018Review
- Importin alpha associates with membranes and participates in nuclear envelope assembly in vitro.The EMBO journal · 2004Article
- Evidence for separable functions of Srp1p, the yeast homolog of importin alpha (Karyopherin alpha): role for Srp1p and Sts1p in protein degradation.Molecular and cellular biology · 2000Article
- Human proliferation-related protein p120 interacts with HSRP1.Chromosoma · 1997Article
- Nucleocytoplasmic transport of macromolecules.Microbiology and molecular biology reviews : MMBR · 1997Review
- Importin alpha from Arabidopsis thaliana is a nuclear import receptor that recognizes three classes of import signals.Plant physiology · 1997Article
- In vivo nuclear transport kinetics in Saccharomyces cerevisiae: a role for heat shock protein 70 during targeting and translocation.The Journal of cell biology · 1996Article
- Stimulation of nuclear import by simian virus 40-transformed cell extracts is dependent on protein kinase activity.Molecular and cellular biology · 1995Article
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4 authors at 1 institution in 1 country.
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Abstract
Srp1p, the protein encoded by SRP1 of Saccharomyces cerevisiae, is a nuclear-pore-associated protein. Its Xenopus homolog, importin, was recently shown to be an essential component required for nuclear localization signal (NLS)-dependent binding of karyophilic proteins to the nuclear envelope [Gorlich, D., Prehn, S., Laskey, R. A. & Hartman, E. (1994) Cell 79, 767-778]. We have discovered a protein kinase whose activity is stimulated by Srp1p (Srp1p fused to glutathione S-transferase and expressed in Escherichia coli) and is detected by phosphorylation of Srp1p and of a 36-kDa protein, a component of the protein kinase complex. The enzyme, called Srp1p kinase, is a protein-serine kinase and was found in extracts in two related complexes of approximately 180 kDa and 220 kDa. The second complex, when purified, contained four protein components including the 36-kDa protein. We observed that, upon purification of the kinase, phosphorylation of Srp1p became very weak, while activation of phosphorylation of the 36-kDa protein by Srp1p remained unaltered. Significantly, NLS peptides and the nuclear proteins we have tested greatly stimulated phosphorylation of Srp1p, suggesting that Srp1p, complexed with karyophilic proteins carrying an NLS, is the in vivo substrate of this protein kinase.
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