ArticleProceedings of the National Academy of Sciences of the United States of America1982
Karyophilic proteins: polypeptides synthesized in vitro accumulate in the nucleus on microinjection into the cytoplasm of amphibian oocytes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1982. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 79 citations in OpenAlex.
- A synthetic snRNA m3G-CAP enhances nuclear delivery of exogenous proteins and nucleic acids.Nucleic acids research · 2009Article
- Cofactor requirements for nuclear export of Rev response element (RRE)- and constitutive transport element (CTE)-containing retroviral RNAs. An unexpected role for actin.The Journal of cell biology · 2001Article
- The vertebrate GLFG nucleoporin, Nup98, is an essential component of multiple RNA export pathways.The Journal of cell biology · 1997Article
- Histone-poly(A) hybrid molecules as tools to block nuclear pores.Journal of protein chemistry · 1995Article
- Localization of the nucleolar protein NO38 in amphibian oocytes.The Journal of cell biology · 1992Article
- Expression of the neuronal noradrenaline transporter in Xenopus laevis oocytes.Naunyn-Schmiedeberg's archives of pharmacology · 1991Article
- Targeting of a chromosomal protein to the nucleus and to lampbrush chromosome loops.Proceedings of the National Academy of Sciences of the United States of America · 1989Article
- Monoclonal antibodies to a Mr 68,000 pore complex glycoprotein interfere with nuclear protein uptake in Xenopus oocytes.Chromosoma · 1988Article
- A monoclonal antibody against the nuclear pore complex inhibits nucleocytoplasmic transport of protein and RNA in vivo.The Journal of cell biology · 1988Article
- Identification of domains involved in nuclear uptake and histone binding of protein N1 of Xenopus laevis.The EMBO journal · 1988Article
- The function of the nuclear envelope in nuclear protein accumulation.The Journal of cell biology · 1988Article
- Article
- Purification of a novel, nucleoplasmin-like protein from somatic nuclei.The EMBO journal · 1987Article
- A constitutive nucleolar protein identified as a member of the nucleoplasmin family.The EMBO journal · 1987Article
- Permeability measurements with closed vesicles from rat liver nuclear envelopes.Proceedings of the National Academy of Sciences of the United States of America · 1987Article
- Preparation and characterization of nuclear-envelope vesicles from rat liver nuclei.The Biochemical journal · 1987Article
- Nuclear-envelope vesicles as a model system to study nucleocytoplasmic transport. Specific uptake of nuclear proteins.The Biochemical journal · 1987Article
- Molecular characterization of a karyophilic, histone-binding protein: cDNA cloning, amino acid sequence and expression of nuclear protein N1/N2 of Xenopus laevis.The EMBO journal · 1986Article
- Determination of the intracellular state of soluble macromolecules by gel filtration in vivo in the cytoplasm of amphibian oocytes.The Journal of cell biology · 1986Article
- Biogenesis of the nuclear lamina: in vivo synthesis and processing of nuclear protein precursors.Proceedings of the National Academy of Sciences of the United States of America · 1986Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The specific nucleocytoplasmic compartmentalization of proteins has been examined for some major soluble acidic nuclear proteins in oocytes of different amphibia. Proteins synthesized and radioactively labeled by translation in vitro, by using mRNA from ovaries of the frog Xenopus laevis, were injected into the cytoplasm of living oocytes of Xenopus or of the salamander Pleurodeles waltlii. At various times after injection, nucleus and cytoplasm were manually separated and endogenous and injected proteins were analyzed by two-dimensional gel electrophoresis. We show that several major nucleus-specific proteins of different sizes and electrical charges, including the very acidic proteins N1 and N2 (Mr, 110,000 and 100,000) and N4 (Mr, 34,000), are identical in both forms--i.e., as translation products in vitro and as present in the nucleoplasm. We conclude that significantly different cytoplasmic precursor forms to these nuclear proteins do not exist. The experiments indicate that (i) the translation products contain the signal(s) directing the specific sequestration of these proteins within the nucleus, (ii) post-translational processing is not required for the accumulation of these proteins in the nucleoplasm, and (iii) the signals and the mechanisms involved are not species specific.
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