| pubmed-article:19893491 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19893491 | lifeskim:mentions | umls-concept:C0041348 | lld:lifeskim |
| pubmed-article:19893491 | lifeskim:mentions | umls-concept:C0441889 | lld:lifeskim |
| pubmed-article:19893491 | lifeskim:mentions | umls-concept:C0449258 | lld:lifeskim |
| pubmed-article:19893491 | lifeskim:mentions | umls-concept:C1333895 | lld:lifeskim |
| pubmed-article:19893491 | lifeskim:mentions | umls-concept:C1413850 | lld:lifeskim |
| pubmed-article:19893491 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:19893491 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:19893491 | pubmed:dateCreated | 2010-1-6 | lld:pubmed |
| pubmed-article:19893491 | pubmed:abstractText | CYLD is a tumour-suppressor gene that is mutated in a benign skin tumour syndrome called cylindromatosis. The CYLD gene product is a deubiquitinating enzyme that was shown to regulate cell proliferation, cell survival and inflammatory responses, mainly through inhibiting NF-kappaB signalling. Here we show that CYLD controls cell growth and division at the G(1)/S-phase as well as cytokinesis by associating with alpha-tubulin and microtubules through its CAP-Gly domains. Translocation of activated CYLD to the perinuclear region of the cell is achieved by an inhibitory interaction of CYLD with histone deacetylase-6 (HDAC6) leading to an increase in the levels of acetylated alpha-tubulin around the nucleus. This facilitates the interaction of CYLD with Bcl-3, leading to a significant delay in the G(1)-to-S-phase transition. Finally, CYLD also interacts with HDAC6 in the midbody where it regulates the rate of cytokinesis in a deubiquitinase-independent manner. Altogether these results identify a mechanism by which CYLD regulates cell proliferation at distinct cell-cycle phases. | lld:pubmed |
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| pubmed-article:19893491 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19893491 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19893491 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19893491 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19893491 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19893491 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19893491 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19893491 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:19893491 | pubmed:issn | 1460-2075 | lld:pubmed |
| pubmed-article:19893491 | pubmed:author | pubmed-author:FässlerReinha... | lld:pubmed |
| pubmed-article:19893491 | pubmed:author | pubmed-author:KhochbinSaadi... | lld:pubmed |
| pubmed-article:19893491 | pubmed:author | pubmed-author:MassoumiRamin... | lld:pubmed |
| pubmed-article:19893491 | pubmed:author | pubmed-author:WickströmSara... | lld:pubmed |
| pubmed-article:19893491 | pubmed:author | pubmed-author:MasoumiKatarz... | lld:pubmed |
| pubmed-article:19893491 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19893491 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:19893491 | pubmed:volume | 29 | lld:pubmed |
| pubmed-article:19893491 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19893491 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19893491 | pubmed:pagination | 131-44 | lld:pubmed |
| pubmed-article:19893491 | pubmed:dateRevised | 2010-9-28 | lld:pubmed |
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