Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-3-1
pubmed:databankReference
pubmed:abstractText
In a genetic screen for nucleoporin-interacting components, a novel nuclear pore protein Nup84p, which exhibits homology to mammalian Nup107p, was isolated. Nup84p forms a complex with five proteins, of which Nup120p, Nup85p, Sec13p, and a Sec13p homolog were identified. Upon isolation of Sec13p-ProtA, nucleoporins were still associated, but the major copurifying band was a 150 kDa protein, showing that Sec13p occurs in two complexes. Disruption of any of the genes encoding Nup84p, Nup85p, or Nup120p caused defects in nuclear membrane and nuclear pore complex organization, as well as in poly(A)+ RNA transport. Thus, the Nup84p complex in conjunction with Sec13-type proteins is required for correct nuclear pore biogenesis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Carboxypeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin A, http://linkedlifedata.com/resource/pubmed/chemical/Epitopes, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Pore Complex Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Poly A, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-myc, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/SEC13 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Staphylococcal Protein A
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
84
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
265-75
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:8565072-Amino Acid Sequence, pubmed-meshheading:8565072-Biological Transport, pubmed-meshheading:8565072-Carboxypeptidases, pubmed-meshheading:8565072-Cathepsin A, pubmed-meshheading:8565072-Epitopes, pubmed-meshheading:8565072-Fungal Proteins, pubmed-meshheading:8565072-Membrane Proteins, pubmed-meshheading:8565072-Molecular Sequence Data, pubmed-meshheading:8565072-Molecular Weight, pubmed-meshheading:8565072-Nuclear Envelope, pubmed-meshheading:8565072-Nuclear Pore Complex Proteins, pubmed-meshheading:8565072-Nuclear Proteins, pubmed-meshheading:8565072-Poly A, pubmed-meshheading:8565072-Proto-Oncogene Proteins c-myc, pubmed-meshheading:8565072-Recombinant Fusion Proteins, pubmed-meshheading:8565072-Saccharomyces cerevisiae Proteins, pubmed-meshheading:8565072-Sequence Homology, Amino Acid, pubmed-meshheading:8565072-Staphylococcal Protein A, pubmed-meshheading:8565072-Yeasts
pubmed:year
1996
pubmed:articleTitle
A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores.
pubmed:affiliation
European Molecular Biology Laboratory, Heidelberg Federal Republic of Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't