Document Detail


Cell cycle phase-dependent changes of localization and oligomerization states of nucleophosmin / B23.
MedLine Citation:
PMID:  8526928     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Nucleophosmin / B23, an abundant nucleolar phosphoprotein, accumulates in the nucleoplasm of cells during the stationary phase of growth or after exposure to selected cytotoxic drugs [Chan, P.K. (1992) Exp. Cell Res. 203, 174-181]. Monomeric and hexameric forms of nucleophosmin / B23 are present in cells [Yung, B.Y.M. and Chan, P.K. (1987) Biochim. Biophys. Acta. 925, 74-82]. Using indirect immunofluorescence, here we show that there are changes in nucleophosmin / B23's cellular localizations throughout the cell cycle. The alternation of the nuclear and nucleolar localizations of nucleophosmin / B23 is most frequently observed in cells of G1 and G1/S phases. The incidence of the changes of localizations of nucleophosmin / B23 decreases as cells enter into S and G2 phases. In parallel, using Western blotting, the reversible change of oligomerization states between the hexameric and monomeric forms of nucleophosmin / B23 is also found to occur most frequently in cells of G1 and G1/S phases. As cells progressed into S, G2 and M phases, the frequency of the reversible change of hexameric and monomeric forms of nucleophosmin / B23 decreases. These findings suggest that nucleophosmin / B23 being possibly involved in rRNA processing and transport, is highly active at G1 and G1/S phases as demonstrated by the dynamic, reversible changes of localization and oligomerization states of nucleophosmin / B23.
Authors:
Y H Chou; B Y Yung
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  217     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  1995 Dec 
Date Detail:
Created Date:  1996-01-19     Completed Date:  1996-01-19     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  313-25     Citation Subset:  IM    
Affiliation:
Department of Pharmacology, Chang Gung Medical & Engineering College, Tao-Yuan, Taiwan, Republic of China.
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MeSH Terms
Descriptor/Qualifier:
Biological Transport, Active
Cell Cycle / physiology*
Cell Nucleolus / metabolism
Cell Nucleus / metabolism
Fluorescent Antibody Technique, Indirect
Hela Cells
Humans
Nuclear Proteins / chemistry,  metabolism*
Phosphoproteins / chemistry,  metabolism*
Protein Conformation
RNA Processing, Post-Transcriptional
RNA, Ribosomal / metabolism
Chemical
Reg. No./Substance:
0/Nuclear Proteins; 0/Phosphoproteins; 0/RNA, Ribosomal; 117896-08-9/nucleophosmin

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