Document Detail


Latrunculin B or ATP depletion induces cofilin-dependent translocation of actin into nuclei of mast cells.
MedLine Citation:
PMID:  12566455     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Increasing cellular G-actin, using latrunculin B, in either intact or permeabilized rat peritoneal mast cells, caused translocation of both actin and an actin regulatory protein, cofilin, into the nuclei. The effect was not associated with an increase in the proportion of apoptotic cells. The major part of the nuclear actin was not stained by rhodamine-phalloidin but could be visualized with an actin antibody, indicating its monomeric or a conformationally distinct state, e.g. cofilin-decorated filaments. Introduction of anti-cofilin into permeabilized cells inhibited nuclear actin accumulation, implying that an active, cofilin-dependent, import exists in this system. Nuclear actin was localized outside the ethidium bromide-stained region, in the extrachromosomal nuclear domain. In permeabilized cells, the appearance of nuclear actin and cofilin was not significantly affected by increasing [Ca(2+)] and/or adding guanosine 5'-O-(3-thiotriphosphate), but was greatly promoted when ATP was withdrawn. Similarly, ATP depletion in intact cells also induced nuclear actin accumulation. In contrast to the effects of latrunculin B, ATP depletion was associated with an increase in cortical F-actin. Our results suggest that the presence of actin in the nucleus may be required for certain stress-induced responses and that cofilin is essential for the nuclear import of actin.
Authors:
Annmarie Pendleton; Brian Pope; Alan Weeds; Anna Koffer
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2003-02-03
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  278     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2003 Apr 
Date Detail:
Created Date:  2003-04-14     Completed Date:  2003-05-22     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  14394-400     Citation Subset:  IM    
Affiliation:
Physiology Department, University College London, University Street, United Kingdom.
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MeSH Terms
Descriptor/Qualifier:
Actin Depolymerizing Factors
Actins / metabolism*
Active Transport, Cell Nucleus
Adenosine Triphosphate / metabolism*
Animals
Apoptosis
Bicyclo Compounds, Heterocyclic / pharmacology*
Calcium / metabolism
Cell Nucleus / metabolism
Cells, Cultured
Flow Cytometry
Fluorescent Dyes / pharmacology
Marine Toxins / pharmacology
Mast Cells / metabolism*
Microfilament Proteins / metabolism*
Microscopy, Confocal
Phalloidine / pharmacology
Protein Conformation
Rats
Rhodamines / pharmacology
Thiazoles / pharmacology*
Thiazolidines
Chemical
Reg. No./Substance:
0/Actin Depolymerizing Factors; 0/Actins; 0/Bicyclo Compounds, Heterocyclic; 0/Fluorescent Dyes; 0/Marine Toxins; 0/Microfilament Proteins; 0/Rhodamines; 0/Thiazoles; 0/Thiazolidines; 17466-45-4/Phalloidine; 56-65-5/Adenosine Triphosphate; 7440-70-2/Calcium; 76343-94-7/latrunculin B

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


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