Document Detail


Nuclear import of protein kinase C occurs by a mechanism distinct from the mechanism used by proteins with a classical nuclear localization signal.
MedLine Citation:
PMID:  9625745     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Protein kinase C does not have any known nuclear localization signal but, nevertheless, is redistributed from the cytoplasm to the nucleus upon various stimuli. In NIH 3T3 fibroblasts stimulation with phorbol ester leads to a translocation of protein kinase C alpha to the plasma membrane and into the cell nucleus. We compared the mechanism of protein kinase C alpha's transport into the nucleus with the transport mechanism of a protein with a classical nuclear localization signal at several steps. To this end, we co-microinjected fluorescently labeled bovine serum albumin to which a nuclear localization signal peptide was coupled, together with substances interfering with conventional nuclear protein import. Thereafter, the distribution of both the nuclear localization signal-bearing reporter protein and protein kinase C alpha was analyzed in the same cells. We can show that, in contrast to the nuclear localization signal-dependent transport, the phorbol ester-induced transport of protein kinase C alpha is not affected by microinjection of antibodies against the nuclear import factor p97/importin/karyopherin beta or microinjection of non-hydrolyzable GTP-analogs. This suggests that nuclear import of protein kinase C alpha is independent of p97/importin/karyopherin beta and independent of GTP. At the nuclear pore there are differences between the mechanisms too, since nuclear transport of protein kinase C alpha cannot be inhibited by wheat germ agglutinin or an antibody against nuclear pore complex proteins. Together these findings demonstrate that the nuclear import of protein kinase C alpha occurs by a mechanism distinct from the one used by classical nuclear localization signal-bearing proteins at several stages.
Authors:
D Schmalz; F Hucho; K Buchner
Related Documents :
11078745 - Alpha-synuclein is phosphorylated by members of the src family of protein-tyrosine kina...
21768135 - Active transport and heat.
11343695 - Cloricromene, a semi-synthetic coumarin derivative, inhibits tumor necrosis factor-alph...
18562315 - Serine 129 phosphorylation of alpha-synuclein induces unfolded protein response-mediate...
1576665 - Effects of isoflavone compounds on the activation of phospholipase c.
16111655 - Lysophosphatidic acid mediates pleiotropic responses in skeletal muscle cells.
Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of cell science     Volume:  111 ( Pt 13)     ISSN:  0021-9533     ISO Abbreviation:  J. Cell. Sci.     Publication Date:  1998 Jul 
Date Detail:
Created Date:  1999-02-23     Completed Date:  1999-02-23     Revised Date:  2012-06-25    
Medline Journal Info:
Nlm Unique ID:  0052457     Medline TA:  J Cell Sci     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  1823-30     Citation Subset:  IM    
Affiliation:
Institut für Biochemie der Freien Universität Berlin, Arbeitsgruppe Neurochemie, Thielallee 63, Germany.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
3T3 Cells
Animals
Biological Transport, Active / drug effects
Cell Nucleus / enzymology
Cytoskeleton / enzymology
Diffusion
Isoenzymes / metabolism*
Mice
Nuclear Localization Signals / drug effects,  physiology*
Nuclear Proteins / physiology
Protein Kinase C / metabolism*
Protein Kinase C-alpha
alpha Karyopherins
beta Karyopherins
ran GTP-Binding Protein
Chemical
Reg. No./Substance:
0/Isoenzymes; 0/Nuclear Localization Signals; 0/Nuclear Proteins; 0/alpha Karyopherins; 0/beta Karyopherins; EC 2.7.11.13/Prkca protein, mouse; EC 2.7.11.13/Protein Kinase C; EC 2.7.11.13/Protein Kinase C-alpha; EC 3.6.5.2/ran GTP-Binding Protein

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  The single CH domain of calponin is neither sufficient nor necessary for F-actin binding.
Next Document:  Actomyosin motor in the merozoite of the malaria parasite, Plasmodium falciparum: implications for r...