pubmed-article:19154724 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19154724 | lifeskim:mentions | umls-concept:C0025266 | lld:lifeskim |
pubmed-article:19154724 | lifeskim:mentions | umls-concept:C0085304 | lld:lifeskim |
pubmed-article:19154724 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
pubmed-article:19154724 | lifeskim:mentions | umls-concept:C0127527 | lld:lifeskim |
pubmed-article:19154724 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
pubmed-article:19154724 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
pubmed-article:19154724 | lifeskim:mentions | umls-concept:C0443211 | lld:lifeskim |
pubmed-article:19154724 | lifeskim:mentions | umls-concept:C0332514 | lld:lifeskim |
pubmed-article:19154724 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:19154724 | pubmed:dateCreated | 2009-1-21 | lld:pubmed |
pubmed-article:19154724 | pubmed:abstractText | Components of the mitotic exit network (MEN), a signaling pathway that triggers exit from mitosis, localize to the spindle pole body (SPB) that migrates into the daughter cell during anaphase but are largely absent from the SPB that remains in the mother cell. Through the analysis of one of the determinants of this asymmetry, Bfa1, we find that the machinery responsible for establishing cell polarity and cytoplasmic microtubules collaborate to establish MEN asymmetry. In cells defective in the Cdc42 signaling pathway or the formin Bni1, Bfa1 localizes to both SPBs. The quantitative analysis of Bfa1 localization further shows that Bfa1 can associate with both SPBs in a transient and highly dynamic fashion, but the protein is stabilized on the SPB that migrates into the daughter cell during anaphase through microtubule-bud cortex interactions. Our results indicate that mother-daughter cell asymmetry determinants establish MEN signaling asymmetry through microtubule-bud cortex interactions. | lld:pubmed |
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pubmed-article:19154724 | pubmed:language | eng | lld:pubmed |
pubmed-article:19154724 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19154724 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:19154724 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:19154724 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19154724 | pubmed:month | Jan | lld:pubmed |
pubmed-article:19154724 | pubmed:issn | 1878-1551 | lld:pubmed |
pubmed-article:19154724 | pubmed:author | pubmed-author:AmonAngelikaA | lld:pubmed |
pubmed-article:19154724 | pubmed:author | pubmed-author:Monje-CasasFe... | lld:pubmed |
pubmed-article:19154724 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:19154724 | pubmed:volume | 16 | lld:pubmed |
pubmed-article:19154724 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19154724 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19154724 | pubmed:pagination | 132-45 | lld:pubmed |
pubmed-article:19154724 | pubmed:dateRevised | 2010-10-4 | lld:pubmed |
pubmed-article:19154724 | pubmed:meshHeading | pubmed-meshheading:19154724... | lld:pubmed |
pubmed-article:19154724 | pubmed:meshHeading | pubmed-meshheading:19154724... | lld:pubmed |
pubmed-article:19154724 | pubmed:meshHeading | pubmed-meshheading:19154724... | lld:pubmed |