ArticleProceedings of the National Academy of Sciences of the United States of America1992
Casein kinase II protein kinase is bound to lamina-matrix and phosphorylates lamin-like protein in isolated pea nuclei.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 66 citations in OpenAlex.
- Review
- Lamin A to Z in normal aging.Aging · 2022Article
- Nuclear lamina CRWN proteins regulate chromatin organization, gene expression, and nuclear body formation in plants.Journal of plant research · 2020Article
- Lamin A buffers CK2 kinase activity to modulate aging in a progeria mouse model.Science advances · 2019Article
- Emerging roles of protein kinase CK2 in abscisic acid signaling.Frontiers in plant science · 2015Review
- The intriguing plant nuclear lamina.Frontiers in plant science · 2014Review
- Functional organization and dynamics of the cell nucleus.Frontiers in plant science · 2014Review
- NMCP/LINC proteins: putative lamin analogs in plants?Plant signaling & behavior · 2013Review
- Dynamics of the plant nuclear envelope and nuclear pore.Plant physiology · 2012Review
- The Arabidopsis nuclear pore and nuclear envelope.The arabidopsis book · 2010Article
- Biochemical and immunological characterization of pea nuclear intermediate filament proteins.Planta · 2004Article
- The plant nuclear envelope.Planta · 2004Review
- Pea DNA topoisomerase I is phosphorylated and stimulated by casein kinase 2 and protein kinase C.Plant physiology · 2003Article
- Distinctive features of plant protein kinase CK2.Molecular and cellular biochemistry · 2001Article
- Characterization, subcellular localization and nuclear targeting of casein kinase 2 from Zea mays.Plant molecular biology · 1999Article
- Association of poly(ADP-ribose) polymerase with nuclear subfractions catalyzed with sodium tetrathionate and hydrogene peroxide crosslinks.Molecular and cellular biochemistry · 1996Article
- Changes in Protein Isoprenylation during the Growth of Suspension-Cultured Tobacco Cells.Plant physiology · 1995Article
- Isolation of an Arabidopsis thaliana casein kinase II beta subunit by complementation in Saccharomyces cerevisiae.Plant molecular biology · 1994Article
- Casein Kinase II-Type Protein Kinase from Pea Cytoplasm and Its Inactivation by Alkaline Phosphatase in Vitro.Plant physiology · 1993Article
- The major nucleoside triphosphatase in pea (Pisum sativum L.) nuclei and in rat liver nuclei share common epitopes also present in nuclear lamins.Plant physiology · 1993Article
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2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
A casein kinase II (CK II)-like protein kinase was identified and partially isolated from a purified envelope-matrix fraction of pea (Pisum sativum L.) nuclei. When [gamma-32P]ATP was directly added to the envelope-matrix preparation, the three most heavily labeled protein bands had molecular masses near 71, 48, and 46 kDa. Protein kinases were removed from the preparation by sequential extraction with Triton X-100, EGTA, 0.3 M NaCl, and a pH 10.5 buffer, but an active kinase still remained bound to the remaining lamina-matrix fraction after these treatments. This kinase had properties resembling CK II kinases previously characterized from animal and plant sources: it preferred casein as an artificial substrate, could use GTP as efficiently as ATP as the phosphoryl donor, was stimulated by spermine, was calcium independent, and had a catalytic subunit of 36 kDa. Some animal and plant CK II kinases have regulatory subunits near 29 kDa, and a lamina-matrix-bound protein of this molecular mass was recognized on immunoblot by anti-Drosophila CK II polyclonal antibodies. Also found associated with the envelope-matrix fraction of pea nuclei were p34cdc2-like and Ca(2+)-dependent protein kinases, but their properties could not account for the protein kinase activity bound to the lamina. The 71-kDa substrate of the CK II-like kinase was lamin A-like, both in its molecular mass and in its cross-reactivity with anti-intermediate filament antibodies. Lamin phosphorylation is considered a crucial early step in the entry of cells into mitosis, so lamina-bound CK II kinases may be important control points for cellular proliferation.
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