RGD Reference Report - Molecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteins. - Rat Genome Database

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Molecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteins.

Authors: Hu, T  Guan, T  Gerace, L 
Citation: Hu T, etal., J Cell Biol 1996 Aug;134(3):589-601.
RGD ID: 633404
Pubmed: PMID:8707840   (View Abstract at PubMed)
PMCID: PMC2120945   (View Article at PubMed Central)

Macromolecular trafficking across the nuclear envelope involves interactions between cytosolic transport factors and nuclear pore complex proteins. The p62 complex, an assembly of 62, 58, 54, and 45-kD O-linked glycoproteins-localized near the central gated channel of the nuclear pore complex, has been directly implicated in nuclear protein import. The cDNA cloning of rat p62 was reported previously. We have now carried out cDNA cloning of rat p58, p54, and p45. We found that p58 contains regions with FG (Phe, Gly) and PA (Pro, Ala) repeats at both its NH2 and COOH termini separated by a predicted alpha-helical coiled-coil region, while p54 has an NH2-terminal FG and PA repeat region and a COOH-terminal predicted coiled-coil region. p45 and p58 appear to be generated by alternative splicing, with p45 containing the NH2-terminal FG repeat region and the coiled-coil region of p58. Using immunogold electron microscopy, we found that p58/p45 and p54 are localized on both sides of the nuclear pore complex, like p62. Previous studies have shown that immobilized recombinant p62 can bind the cytosolic nuclear import factor NTF2 and thereby deplete transport activity from cytosol. We have now found that immobilized recombinant p58 and p54 also can deplete nuclear transport activity from cytosol, and that p62, p58, and p54 bind directly to the cytosolic nuclear import factors p97 and NTF2. At least in the case of p58, this involves FG repeat regions. Moreover, p58 can bind to a complex containing transport ligand, the nuclear localization sequence receptor (Srp1 alpha) and p97. These data support a model in which the p62 complex binds to a multicomponent particle consisting of transport ligand and cytosolic factors to achieve accumulation of ligand near the central gated channel of the nuclear pore complex.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Nup54Ratnucleocytoplasmic transport involved_inIDA PMID:8707840UniProt 
Nup58Ratnucleocytoplasmic transport involved_inIDA PMID:8707840UniProt 
Nup54Ratprotein targeting involved_inIDA PMID:8707840UniProt 
Nup54Ratregulation of protein import into nucleus  IDA  RGD 
Nup58Ratregulation of protein import into nucleus  IDA  RGD 
Nup62Ratregulation of protein import into nucleus  IDA  RGD 

Cellular Component

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Nup54Ratnuclear envelope  IDA  RGD 
Nup54Ratnuclear pore part_ofIDA PMID:8707840UniProt 
Nup58Ratnuclear pore part_ofIDA PMID:8707840UniProt 

Objects Annotated

Genes (Rattus norvegicus)
Kpnb1  (karyopherin subunit beta 1)
Nup54  (nucleoporin 54)
Nup58  (nucleoporin 58)
Nup62  (nucleoporin 62)
Nutf2  (nuclear transport factor 2)

Objects referenced in this article
Gene NUP54 nucleoporin 54 Homo sapiens
Gene Nup58_v1 nucleoporin 58, variant 1 Rattus norvegicus
Gene Nup58_v2 nucleoporin 58, variant 2 Rattus norvegicus

Additional Information