Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2007-2-9
pubmed:abstractText
Export of mature mRNA to the cytoplasm is the culmination of the nuclear portion of eukaryotic gene expression. After transport-competent mature mRNP export complexes are formed in the nucleus, their passage through nuclear pore complexes (NPCs) is facilitated by the Mex67:Mtr2 heterodimer. At the NPC cytoplasmic face, mRNP remodeling prevents its return to the nucleus and so functions as a molecular ratchet imposing directionality on transport. In budding yeast, recent work suggests that the DEAD-box helicase Dbp5 remodels mRNPs at the NPC cytoplasmic face by removing Mex67 and that the Dbp5 ATPase is activated by Gle1 and inositol hexaphosphate (IP(6)).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DBP5 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/DEAD-box RNA Helicases, http://linkedlifedata.com/resource/pubmed/chemical/GLE1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/MEX67 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Mtr2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Pore Complex Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nucleocytoplasmic Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phytic Acid, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/RNA Helicases, http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/messenger ribonucleoprotein
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1097-2765
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
327-30
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:17289581-Active Transport, Cell Nucleus, pubmed-meshheading:17289581-Carrier Proteins, pubmed-meshheading:17289581-Cell Nucleus, pubmed-meshheading:17289581-DEAD-box RNA Helicases, pubmed-meshheading:17289581-Dimerization, pubmed-meshheading:17289581-Membrane Transport Proteins, pubmed-meshheading:17289581-Models, Biological, pubmed-meshheading:17289581-Nuclear Pore Complex Proteins, pubmed-meshheading:17289581-Nuclear Proteins, pubmed-meshheading:17289581-Nucleocytoplasmic Transport Proteins, pubmed-meshheading:17289581-Phytic Acid, pubmed-meshheading:17289581-Protein Processing, Post-Translational, pubmed-meshheading:17289581-RNA, Messenger, pubmed-meshheading:17289581-RNA Helicases, pubmed-meshheading:17289581-RNA-Binding Proteins, pubmed-meshheading:17289581-Ribonucleoproteins, pubmed-meshheading:17289581-Saccharomyces cerevisiae Proteins
pubmed:year
2007
pubmed:articleTitle
Ratcheting mRNA out of the nucleus.
pubmed:affiliation
MRC Laboratory of Molecular Biology, Hills Road, Cambridge, UK. ms@mrc-lmb.cam.ac.uk
pubmed:publicationType
Journal Article, Review