| pubmed-article:16314522 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16314522 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:16314522 | lifeskim:mentions | umls-concept:C0005528 | lld:lifeskim |
| pubmed-article:16314522 | lifeskim:mentions | umls-concept:C0034800 | lld:lifeskim |
| pubmed-article:16314522 | lifeskim:mentions | umls-concept:C0521447 | lld:lifeskim |
| pubmed-article:16314522 | lifeskim:mentions | umls-concept:C1550548 | lld:lifeskim |
| pubmed-article:16314522 | lifeskim:mentions | umls-concept:C1555714 | lld:lifeskim |
| pubmed-article:16314522 | lifeskim:mentions | umls-concept:C1705654 | lld:lifeskim |
| pubmed-article:16314522 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:16314522 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:16314522 | pubmed:dateCreated | 2005-11-29 | lld:pubmed |
| pubmed-article:16314522 | pubmed:abstractText | The cell membrane receptor ErbB-2 migrates to the nucleus. However, the mechanism of its nuclear translocation is unclear. Here, we report a novel mechanism of its nuclear localization that involves interaction with the transport receptor importin beta1, nuclear pore protein Nup358, and a host of players in endocytic internalization. Knocking down importin beta1 using small interfering RNA oligonucleotides or inactivation of small GTPase Ran by RanQ69L, a dominant-negative mutant of Ran, causes a nuclear transport defect of ErbB-2. Mutation of a putative nuclear localization signal in ErbB-2 destroys its interaction with importin beta1 and arrests nuclear translocation, while inactivation of nuclear export receptor piles up ErbB-2 within the nucleus. Additionally, blocking of internalization by a dominant-negative mutant of dynamin halts its nuclear localization. Thus, the cell membrane-embedded ErbB-2, through endocytosis using the endocytic vesicle as a vehicle, importin beta1 as a driver and Nup358 as a traffic light, migrates from the cell surface to the nucleus. This novel mechanism explains how a receptor tyrosine kinase on the cell surface can be translocated into the nucleus. This pathway may serve as a general mechanism to allow direct communication between cell surface receptors and the nucleus, and our findings thus open a new era in understanding direct trafficking between the cell membrane and nucleus. | lld:pubmed |
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| pubmed-article:16314522 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16314522 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16314522 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16314522 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16314522 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:16314522 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:16314522 | pubmed:author | pubmed-author:PengB KBK | lld:pubmed |
| pubmed-article:16314522 | pubmed:author | pubmed-author:WangShao-Chun... | lld:pubmed |
| pubmed-article:16314522 | pubmed:author | pubmed-author:HungMien-Chie... | lld:pubmed |
| pubmed-article:16314522 | pubmed:author | pubmed-author:Bartholomeusz... | lld:pubmed |
| pubmed-article:16314522 | pubmed:author | pubmed-author:LeeDung-FangD... | lld:pubmed |
| pubmed-article:16314522 | pubmed:author | pubmed-author:LiLong-YuanLY | lld:pubmed |
| pubmed-article:16314522 | pubmed:author | pubmed-author:Ali-SeyedMoha... | lld:pubmed |
| pubmed-article:16314522 | pubmed:author | pubmed-author:GiriDipak KDK | lld:pubmed |
| pubmed-article:16314522 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16314522 | pubmed:volume | 25 | lld:pubmed |
| pubmed-article:16314522 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16314522 | pubmed:authorsComplete | Y | lld:pubmed |
