| pubmed-article:10397761 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10397761 | lifeskim:mentions | umls-concept:C0038323 | lld:lifeskim |
| pubmed-article:10397761 | lifeskim:mentions | umls-concept:C0040648 | lld:lifeskim |
| pubmed-article:10397761 | lifeskim:mentions | umls-concept:C0299508 | lld:lifeskim |
| pubmed-article:10397761 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:10397761 | lifeskim:mentions | umls-concept:C0439851 | lld:lifeskim |
| pubmed-article:10397761 | lifeskim:mentions | umls-concept:C0887839 | lld:lifeskim |
| pubmed-article:10397761 | lifeskim:mentions | umls-concept:C0178499 | lld:lifeskim |
| pubmed-article:10397761 | lifeskim:mentions | umls-concept:C0332256 | lld:lifeskim |
| pubmed-article:10397761 | lifeskim:mentions | umls-concept:C0220905 | lld:lifeskim |
| pubmed-article:10397761 | lifeskim:mentions | umls-concept:C1552596 | lld:lifeskim |
| pubmed-article:10397761 | lifeskim:mentions | umls-concept:C1709305 | lld:lifeskim |
| pubmed-article:10397761 | lifeskim:mentions | umls-concept:C1947931 | lld:lifeskim |
| pubmed-article:10397761 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:10397761 | lifeskim:mentions | umls-concept:C0453984 | lld:lifeskim |
| pubmed-article:10397761 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:10397761 | pubmed:dateCreated | 1999-8-27 | lld:pubmed |
| pubmed-article:10397761 | pubmed:abstractText | The sterol regulatory element-binding protein-2 (SREBP-2) is produced as a large precursor molecule attached to the endoplasmic reticulum membrane. In response to the sterol depletion, the N-terminal segment of the precursor, which contains a basic helix-loop-helix-leucine zipper domain, is released by two sequential cleavages and is translocated to the nucleus, where it activates the transcription of target genes. The data herein show that released SREBP-2 uses a distinct nuclear transport pathway, which is mediated by importin beta. The mature form of SREBP-2 is actively transported into the nucleus when injected into the cell cytoplasm. SREBP-2 binds directly to importin beta in the absence of importin alpha. Ran-GTP but not Ran-GDP causes the dissociation of the SREBP-2-importin beta complex. G19VRan-GTP inhibits the nuclear import of SREBP-2 in living cells. In the permeabilized cell in vitro transport system, nuclear import of SREBP-2 is reconstituted only by importin beta in conjunction with Ran and its interacting protein p10/NTF2. We further demonstrate that the helix-loop-helix-leucine zipper motif of SREBP-2 contains a novel type of nuclear localization signal, which binds directly to importin beta. | lld:pubmed |
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| pubmed-article:10397761 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10397761 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10397761 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10397761 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10397761 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10397761 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10397761 | pubmed:status | MEDLINE | lld:pubmed |
