rdf:type |
|
lifeskim:mentions |
umls-concept:C0475264,
umls-concept:C0521447,
umls-concept:C0598988,
umls-concept:C1167622,
umls-concept:C1314939,
umls-concept:C1421545,
umls-concept:C1514562,
umls-concept:C1704675,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
|
pubmed:issue |
16
|
pubmed:dateCreated |
2002-7-24
|
pubmed:abstractText |
Vertebrate tRNA export receptor exportin-t (Xpo-t) binds to RanGTP and mature tRNAs cooperatively to form a nuclear export complex. Xpo-t shuttles bidirectionally through nuclear pore complexes (NPCs) but is mainly nuclear at steady state. The steady-state distribution of Xpo-t is shown to depend on its interaction with RanGTP. Two distinct Xpo-t NPC interaction domains that bind differentially to peripherally localized nucleoporins in vitro are identified. The N terminus binds to both Nup153 and RanBP2/Nup358 in a RanGTP-dependent manner, while the C terminus binds to CAN/Nup214 independently of Ran. We propose that these interactions increase the concentration of tRNA export complexes and of empty Xpo-t in the vicinity of NPCs and thus increase the efficiency of the Xpo-t transport cycle.
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12138183-10199570,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12138183-10202161,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12138183-1827444,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12138183-9930651
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0270-7306
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
22
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
5708-20
|
pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:12138183-Humans,
pubmed-meshheading:12138183-Animals,
pubmed-meshheading:12138183-Xenopus laevis,
pubmed-meshheading:12138183-Protein Binding,
pubmed-meshheading:12138183-RNA, Transfer,
pubmed-meshheading:12138183-Models, Biological,
pubmed-meshheading:12138183-HeLa Cells,
pubmed-meshheading:12138183-Microinjections,
pubmed-meshheading:12138183-Oocytes,
pubmed-meshheading:12138183-Nuclear Proteins,
pubmed-meshheading:12138183-Carrier Proteins,
pubmed-meshheading:12138183-Protein Structure, Tertiary,
pubmed-meshheading:12138183-Nuclear Pore,
pubmed-meshheading:12138183-Active Transport, Cell Nucleus
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