| pubmed-article:18367646 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18367646 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:18367646 | lifeskim:mentions | umls-concept:C0008546 | lld:lifeskim |
| pubmed-article:18367646 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:18367646 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:18367646 | lifeskim:mentions | umls-concept:C0598405 | lld:lifeskim |
| pubmed-article:18367646 | lifeskim:mentions | umls-concept:C1612096 | lld:lifeskim |
| pubmed-article:18367646 | lifeskim:mentions | umls-concept:C0233656 | lld:lifeskim |
| pubmed-article:18367646 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:18367646 | pubmed:dateCreated | 2008-4-16 | lld:pubmed |
| pubmed-article:18367646 | pubmed:abstractText | The Drosophila retinoblastoma family of proteins (RBF1 and RBF2) and their mammalian homologs (pRB, p130, and p107) are best known for their regulation of the G1/S transition via the repression of E2F-dependent transcription. However, RB family members also possess additional functions. Here, we report that rbf1 mutant larvae have extensive defects in chromatin condensation during mitosis. We describe a novel interaction between RBF1 and dCAP-D3, a non-SMC component of the Condensin II complex that links RBF1 to the regulation of chromosome structure. RBF1 physically interacts with dCAP-D3, RBF1 and dCAP-D3 partially colocalize on polytene chromosomes, and RBF1 is required for efficient association of dCAP-D3 with chromatin. dCap-D3 mutants also exhibit chromatin condensation defects, and mutant alleles of dCap-D3 suppress cellular and developmental phenotypes induced by the overexpression of RBF1. Interestingly, this interaction is conserved between flies and humans. The re-expression of pRB into a pRB-deficient human tumor cell line promotes chromatin association of hCAP-D3 in a manner that depends on the LXCXE-binding cleft of pRB. These results uncover an unexpected link between pRB/RBF1 and chromatin condensation, providing a mechanism by which the functional inactivation of RB family members in human tumor cells may contribute to genome instability. | lld:pubmed |
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| pubmed-article:18367646 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18367646 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18367646 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18367646 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18367646 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18367646 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:18367646 | pubmed:issn | 0890-9369 | lld:pubmed |
| pubmed-article:18367646 | pubmed:author | pubmed-author:DysonNicholas... | lld:pubmed |
| pubmed-article:18367646 | pubmed:author | pubmed-author:JiJun-YuanJY | lld:pubmed |
| pubmed-article:18367646 | pubmed:author | pubmed-author:LongworthMich... | lld:pubmed |
| pubmed-article:18367646 | pubmed:author | pubmed-author:HerrAnabelA | lld:pubmed |
| pubmed-article:18367646 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18367646 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:18367646 | pubmed:volume | 22 | lld:pubmed |
| pubmed-article:18367646 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18367646 | pubmed:authorsComplete | Y | lld:pubmed |
