Linked Life Data

3313397

Source:http://linkedlifedata.com/resource/pubmed/id/3313397

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
1987-12-9
pubmed:abstractText
Using a monoclonal antibody (mAb 414), we previously identified a protein of 62 kDa (p62) that was localized to the nuclear pore complex by immunoelectron microscopy. We also showed that p62 binds specifically to wheat germ agglutinin. Therefore, we proposed that this nuclear pore complex protein might be a member of a recently characterized family of glycoproteins that are labeled by in vitro galactosylation of rat liver nuclei and contain O-linked monosaccharidic GlcNAc residues. In support of this, we now show that incubation with N-acetylglucosaminidase reduces the molecular mass of p62 by approximately 3 kDa because of the removal of terminal GlcNAc residues. Moreover, p62 can be galactosylated in vitro by using UDP-[3H]galactose and galactosyltransferase. We also show that most of the GlcNAc residues are added within 5 min of synthesis, when p62 is soluble and cytosolic. Thus, the addition of GlcNAc is carried out in the cytoplasm and is clearly distinct from the N- and O-linked glycosylation pathways of the endoplasmic reticulum and Golgi complex. Using another mAb with a broad specificity for nuclear GlcNAc-containing proteins, we show by immunofluorescence and protein blotting of subnuclear fractions that some of these proteins are in the interior of the nucleus, and others are most likely located in the pore complex.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/3313397-14963, http://linkedlifedata.com/resource/pubmed/commentcorrection/3313397-167767, http://linkedlifedata.com/resource/pubmed/commentcorrection/3313397-2437126, http://linkedlifedata.com/resource/pubmed/commentcorrection/3313397-3086323, http://linkedlifedata.com/resource/pubmed/commentcorrection/3313397-3100529, http://linkedlifedata.com/resource/pubmed/commentcorrection/3313397-320200, http://linkedlifedata.com/resource/pubmed/commentcorrection/3313397-3518946, http://linkedlifedata.com/resource/pubmed/commentcorrection/3313397-3571327, http://linkedlifedata.com/resource/pubmed/commentcorrection/3313397-3805121, http://linkedlifedata.com/resource/pubmed/commentcorrection/3313397-4204552, http://linkedlifedata.com/resource/pubmed/commentcorrection/3313397-5572750, http://linkedlifedata.com/resource/pubmed/commentcorrection/3313397-5924199, http://linkedlifedata.com/resource/pubmed/commentcorrection/3313397-6300906, http://linkedlifedata.com/resource/pubmed/commentcorrection/3313397-6421821, http://linkedlifedata.com/resource/pubmed/commentcorrection/3313397-6784450, http://linkedlifedata.com/resource/pubmed/commentcorrection/3313397-986398
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:volume
84
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7552-6
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Nuclear pore complex contains a family of glycoproteins that includes p62: glycosylation through a previously unidentified cellular pathway.
pubmed:affiliation
Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York, NY 10021.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.