|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
20
|
|
pubmed:dateCreated |
2001-9-26
|
|
pubmed:abstractText |
Peptide:N-glycanase (PNGase) cleaves oligosaccharide chains from glycopeptides and glycoproteins. Recently the deduced amino acid sequence of a cytoplasmic PNGase has been identified in various eukaryotes ranging from yeast to mammals, suggesting that deglycosylation may play a central role in some catabolic process. Several lines of evidence indicate that the cytoplasmic enzyme is involved in the quality control system for newly synthesized glycoproteins. Two-hybrid library screening by using mouse PNGase as the target yielded several PNGase-interacting proteins that previously had been implicated in proteasome-dependent protein degradation: mHR23B, ubiquitin, a regulatory subunit of the 19S proteasome, as well as a protein containing an ubiquitin regulatory motif (UBX) and an ubiquitin-associated motif (UBA). These findings by using the two-hybrid system were further confirmed either by in vitro binding assays or size fractionation assays. These results suggest that PNGase may be required for efficient proteasome-mediated degradation of misfolded glycoproteins in mammalian cells.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-10028183,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-10363658,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-10452618,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-10456327,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-10488153,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-10564637,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-10597633,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-10788493,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-10831608,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-10913188,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-11023840,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-11139575,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-11146622,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-11243799,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-11259433,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-11323716,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-11430818,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-7786020,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-8352768,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-8871400,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-8945469,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-9038332,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-9050876,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-9177196,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-9177202,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-9252124,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-9252404,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-9285707,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-9419209,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-9437001,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-9500786,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-9545309,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-9553052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-9639660,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-9705282,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-9792704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562482-9864362
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Sep
|
|
pubmed:issn |
0027-8424
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
25
|
|
pubmed:volume |
98
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
11163-8
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:11562482-3T3 Cells,
pubmed-meshheading:11562482-Amidohydrolases,
pubmed-meshheading:11562482-Animals,
pubmed-meshheading:11562482-COS Cells,
pubmed-meshheading:11562482-Cercopithecus aethiops,
pubmed-meshheading:11562482-Cloning, Molecular,
pubmed-meshheading:11562482-Cysteine Endopeptidases,
pubmed-meshheading:11562482-Cytoplasm,
pubmed-meshheading:11562482-Escherichia coli,
pubmed-meshheading:11562482-Gene Library,
pubmed-meshheading:11562482-Mammals,
pubmed-meshheading:11562482-Mice,
pubmed-meshheading:11562482-Multienzyme Complexes,
pubmed-meshheading:11562482-Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase,
pubmed-meshheading:11562482-Proteasome Endopeptidase Complex,
pubmed-meshheading:11562482-Proteins,
pubmed-meshheading:11562482-Recombinant Fusion Proteins,
pubmed-meshheading:11562482-Recombinant Proteins,
pubmed-meshheading:11562482-Saccharomyces cerevisiae,
pubmed-meshheading:11562482-Substrate Specificity,
pubmed-meshheading:11562482-Transfection,
pubmed-meshheading:11562482-Ubiquitin
|
|
pubmed:year |
2001
|
|
pubmed:articleTitle |
Identification of proteins that interact with mammalian peptide:N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradation.
|
|
pubmed:affiliation |
Department of Biochemistry, State University of New York, Stony Brook, NY 11794-5215, USA.
|
