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PMID: 8526928 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Cell cycle phase-dependent changes of localization and oligomerization states of nucleophosmin / B23.

Biochemical and biophysical research communications ·Vol. 217 ·No. 1 ·1995-12-05 ·Pages 313-25

Chou YH, Yung BY

Abstract

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.

MeSH Terms
Biological Transport, Active Cell Cycle/physiology Cell Nucleolus/metabolism Cell Nucleus/metabolism Fluorescent Antibody Technique, Indirect HeLa Cells Humans Nuclear Proteins/chemistry,metabolism Nucleophosmin Phosphoproteins/chemistry,metabolism Protein Conformation RNA Processing, Post-Transcriptional RNA, Ribosomal/metabolism
Chemicals
NPM1 protein, human Nuclear Proteins Phosphoproteins RNA, Ribosomal Nucleophosmin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Chou Y H
Department of Pharmacology, Chang Gung Medical & Engineering College, Tao-Yuan, Taiwan, Republic of China.
Yung B Y
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1995-12-05
Pages
313-25
Language
English
Region
United States
NLM ID
0372516
Subset
IM
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