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

1996 ◽  
Vol 317 (1) ◽  
pp. 321-327 ◽  
Author(s):  
Yi-Yi LU ◽  
Chun-Yuen LAM ◽  
Benjamin Yat-Ming YUNG
Keyword(s):  
Protein Kinase ◽  
Hela Cells ◽  
Kinase Inhibitor ◽  
Specific Form ◽  
Protein Kinase Inhibitor ◽  
Condensed State ◽  
Mitotic Chromosomes ◽  
Cdc2 Kinase ◽  
Phosphorylated Form ◽  
Chromosome Decondensation

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.

Evidence For In Vivo Inhibition of CMV Infection by the Quinazoline Class Protein Kinase Inhibitor Gefitinib

2007 ◽  
Vol 74 (3) ◽  
pp. A34-A35
Author(s):  
M SCHLEISS ◽  
M MCVOY ◽  
X CUI ◽  
Y CHOI ◽  
J ANDERSON ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Kinase Inhibitor ◽  
Protein Kinase Inhibitor ◽  
Cmv Infection

Cloning and mapping of human PKIB and PKIG, and comparison of tissue expression patterns of three members of the protein kinase inhibitor family, including PKIA

2000 ◽  
Vol 349 (2) ◽  
pp. 403-407 ◽  
Author(s):  
Lihua ZHENG ◽  
Long YU ◽  
Qiang TU ◽  
Min ZHANG ◽  
Hua HE ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Nuclear Export ◽  
Kinase Inhibitor ◽  
Expression Patterns ◽  
Nuclear Export Signal ◽  
Tissue Expression ◽  
Protein Kinase Inhibitor ◽  
The Other ◽  
Dependent Protein

Two novel members of the human cAMP-dependent protein kinase inhibitor (PKI) gene family, PKIB and PKIG, were cloned. The deduced proteins showed 70% and 90% identity with mouse PKIβ and PKIγ respectively. Both the already identified pseudosubstrate site and leucine-rich nuclear export signal motifs were defined from the 11 PKIs of different species. The PKIB and PKIG genes were mapped respectively to chromosome 6q21-22.1, using a radiation hybrid GB4 panel, and to chromosome 20q13.12-13.13, using a Stanford G3 panel. Northern-blot analysis of three PKI isoforms, including the PKIA identified previously, revealed significant differences in their expression patterns. PKIB had two transcripts of 1.9 kb and 1.4 kb. The former transcript was abundant in both placenta and brain and the latter was expressed most abundantly in placenta, highly in brain, heart, liver, pancreas, moderately in kidney, skeletal muscle and colon, and very little in the other eight tissues tested. PKIG was widely expressed as a 1.5-kb transcript with the highest level in heart, hardly detectable in thymus and peripheral blood leucocytes and was moderately expressed in the other tissues, with slightly different levels. However, PKIA was specifically expressed as two transcripts of 3.3 kb and 1.5 kb in heart and skeletal muscle. The distinct expression patterns of the three PKIs suggest that their roles in various tissues are probably different.

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