rdf:type |
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lifeskim:mentions |
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pubmed:issue |
18
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pubmed:dateCreated |
2009-9-15
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pubmed:abstractText |
Here, we have analyzed the subcellular destiny of newly synthesized tight junction protein zona occludens (ZO)-2. After transfection in sparse cells, 74% of cells exhibit ZO-2 at the nucleus, and after 18 h the value decreases to 17%. The mutation S369A located within the nuclear exportation signal 1 of ZO-2 impairs the nuclear export of the protein. Because Ser369 represents a putative protein kinase C (PKC) phosphorylation site, we tested the effect of PKC inhibition and stimulation on the nuclear export of ZO-2. Our results strongly suggest that the departure of ZO-2 from the nucleus is regulated by phosphorylation at Ser369 by novel PKCepsilon. To test the route taken by ZO-2 from synthesis to the plasma membrane, we devised a novel nuclear microinjection assay in which the nucleus served as a reservoir for anti-ZO-2 antibody. Through this assay, we demonstrate that a significant amount of newly synthesized ZO-2 goes into the nucleus and is later relocated to the plasma membrane. These results constitute novel information for understanding the mechanisms that regulate the intracellular fate of ZO-2.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-10026224,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-10575001,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-10601346,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-10844608,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-10874042,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-10966866,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-11443064,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-11698413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-11716757,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-11855865,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-12403786,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-15194440,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-15616198,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-15975580,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-16920099,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-17142835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-19056685,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-2014265,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-2777783,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-4032460,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-8798776,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-8801352,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19625451-9683540
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Sep
|
pubmed:issn |
1939-4586
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pubmed:author |
pubmed-author:AlarcónLourdesL,
pubmed-author:BandalaYamirY,
pubmed-author:ChamorroDavidD,
pubmed-author:González-AguilarHéctorH,
pubmed-author:González-MariscalLorenzaL,
pubmed-author:JuaristiEusebioE,
pubmed-author:Mejía-CastilloTeresaT,
pubmed-author:PonceArturoA,
pubmed-author:Robles-FloresMarthaM,
pubmed-author:SegoviaJoséJ,
pubmed-author:TapiaRocioR
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pubmed:issnType |
Electronic
|
pubmed:volume |
20
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
4120-9
|
pubmed:dateRevised |
2010-9-27
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pubmed:meshHeading |
pubmed-meshheading:19625451-Active Transport, Cell Nucleus,
pubmed-meshheading:19625451-Animals,
pubmed-meshheading:19625451-Cell Membrane,
pubmed-meshheading:19625451-Cell Nucleus,
pubmed-meshheading:19625451-Dogs,
pubmed-meshheading:19625451-Epithelial Cells,
pubmed-meshheading:19625451-Fatty Acids, Unsaturated,
pubmed-meshheading:19625451-Immunoprecipitation,
pubmed-meshheading:19625451-Membrane Proteins,
pubmed-meshheading:19625451-Mutant Proteins,
pubmed-meshheading:19625451-Phosphorylation,
pubmed-meshheading:19625451-Phosphoserine,
pubmed-meshheading:19625451-Protein Binding,
pubmed-meshheading:19625451-Protein Kinase C-epsilon,
pubmed-meshheading:19625451-Protein Kinase Inhibitors,
pubmed-meshheading:19625451-Time Factors,
pubmed-meshheading:19625451-Transfection
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pubmed:year |
2009
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pubmed:articleTitle |
Phosphorylation of zona occludens-2 by protein kinase C epsilon regulates its nuclear exportation.
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pubmed:affiliation |
Departments of Physiology, Biophysics, and Neuroscience, Center for Research and Advanced Studies (CINVESTAV), Mexico, D.F., 07360, Mexico.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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