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Literature DB >> 8694782

Decreased accumulation and dephosphorylation of the mitosis-specific form of nucleophosmin/B23 in staurosporine-induced chromosome decondensation.

Abstract

Nucleophosmin/B23 is highly phosphorylated by cdc2 kinase during mitosis, and this phosphorylation most probably has a role in initiating and controlling the entry of cells into mitosis [Peter, Nakagawa, Doree, Labbe and Nigg (1990) Cell 60, 791-801]. In the present study, the protein kinase inhibitor staurosporine has been used to examine possible changes in nucleophosmin/B23 at mitosis in HeLa cells. Addition of staurosporine to HeLa cells already arrested at mitosis by nocodazole causes: (i) decreased accumulation of the mitosis-specific form of nucleophosmin/B23, (ii) dephosphorylation of nucleophosmin/ B23, (iii) redistribution of nucleophosmin/B23 to the cytosol, and (iv) concomitant decondensation of chromosomes. These results suggest that the mitosis-specific phosphorylated form of nucleophosmin/B23 may play a role in maintaining mitotic chromosomes in their condensed state.

Entities: Chemical Gene

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Year: 1996 PMID： 8694782 PMCID： PMC1217481 DOI： 10.1042/bj3170321

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

38 in total

1. Short exposure to actinomycin D induces "reversible" translocation of protein B23 as well as "reversible" inhibition of cell growth and RNA synthesis in HeLa cells.

Authors: B Y Yung; A M Bor; P K Chan
Journal: Cancer Res Date: 1990-09-15 Impact factor: 12.701

2. Characterization of specific binding sites for [3H]-staurosporine on various protein kinases.

Authors: J M Herbert; E Seban; J P Maffrand
Journal: Biochem Biophys Res Commun Date: 1990-08-31 Impact factor: 3.575

3. Identification of major nucleolar proteins as candidate mitotic substrates of cdc2 kinase.

Authors: M Peter; J Nakagawa; M Dorée; J C Labbé; E A Nigg
Journal: Cell Date: 1990-03-09 Impact factor: 41.582

4. A nucleolar auto-antigen is part of a major chromosomal surface component.

Authors: Y Yasuda; G G Maul
Journal: Chromosoma Date: 1990-04 Impact factor: 4.316

5. Characterization of the cDNA encoding human nucleophosmin and studies of its role in normal and abnormal growth.

Authors: W Y Chan; Q R Liu; J Borjigin; H Busch; O M Rennert; L A Tease; P K Chan
Journal: Biochemistry Date: 1989-02-07 Impact factor: 3.162

6. The major phosphorylation site of nucleophosmin (B23) is phosphorylated by a nuclear kinase II.

Authors: P K Chan; Q R Liu; E Durban
Journal: Biochem J Date: 1990-09-01 Impact factor: 3.857

7. Specific complex of human immunodeficiency virus type 1 rev and nucleolar B23 proteins: dissociation by the Rev response element.

Authors: C Fankhauser; E Izaurralde; Y Adachi; P Wingfield; U K Laemmli
Journal: Mol Cell Biol Date: 1991-05 Impact factor: 4.272

Decreased accumulation and dephosphorylation of the mitosis-specific form of nucleophosmin/B23 in staurosporine-induced chromosome decondensation.

1. Short exposure to actinomycin D induces "reversible" translocation of protein B23 as well as "reversible" inhibition of cell growth and RNA synthesis in HeLa cells.

2. Characterization of specific binding sites for [3H]-staurosporine on various protein kinases.

3. Identification of major nucleolar proteins as candidate mitotic substrates of cdc2 kinase.

4. A nucleolar auto-antigen is part of a major chromosomal surface component.

5. Characterization of the cDNA encoding human nucleophosmin and studies of its role in normal and abnormal growth.

6. The major phosphorylation site of nucleophosmin (B23) is phosphorylated by a nuclear kinase II.

7. Specific complex of human immunodeficiency virus type 1 rev and nucleolar B23 proteins: dissociation by the Rev response element.

8. Immunolocalization of phosphoprotein B23 in proliferating and non-proliferating HeLa cells.

9. Staurosporine inhibits a tyrosine protein kinase in human hepatoma cell membranes.

10. Cross-linkage of nucleophosmin in tumor cells by nitrogen mustard.

1. Phosphorylation of AIB1 at mitosis is regulated by CDK1/CYCLIN B.