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dc.contributor.authorWalker, AK
dc.contributor.authorSoo, KY
dc.contributor.authorLevina, V
dc.contributor.authorTalbo, GH
dc.contributor.authorAtkin, JD
dc.date.available2014-05-22T08:32:20Z
dc.date.available2012-11-08
dc.date.available2012-11-08
dc.date.available2012-11-08
dc.date.issued2013-01-01
dc.identifierhttp://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000312995400018&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=d4d813f4571fa7d6246bdc0dfeca3a1c
dc.identifier.citationWalker, A. K., Soo, K. Y., Levina, V., Talbo, G. H. & Atkin, J. D. (2013). N-linked glycosylation modulates dimerization of protein disulfide isomerase family A member 2 (PDIA2). FEBS JOURNAL, 280 (1), pp.233-243. https://doi.org/10.1111/febs.12063.
dc.identifier.issn1742-464X
dc.identifier.urihttp://hdl.handle.net/11343/33269
dc.descriptionC1 - Journal Articles Refereed
dc.description.abstractProtein disulfide isomerase (PDI) family members are important enzymes for the correct folding and maturation of proteins that transit or reside in the endoplasmic reticulum (ER). The human PDI family comprises at least 19 members that differ in cell type expression, substrate specificity and post-translational modifications. PDI family A member 2 (PDIA2, previously known as PDIp) has a similar domain structure to prototypical PDI (also known as PDIA1), but the function and post-translational modifications of PDIA2 remain poorly understood. Unlike most PDI family members, PDIA2 contains three predicted N-linked glycosylation sites. By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells. Furthermore, mutation of N284 to glycosylation-null Gln increases formation of a highly stable disulfide-bonded PDIA2 dimer. Nevertheless, in HeLa cells, both wild-type and N127/284/516Q mutant PDIA2 proteins localize to the ER, but not the ER-Golgi intermediate compartment, suggesting that glycosylation is important for PDIA2 protein-protein interactions but not subcellular localization. Finally, we identified human major histocompatibility complex class 1 antigens (HLA-A,B,C) as potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease. These results further characterize this poorly defined member of the PDI family.
dc.formatapplication/pdf
dc.languageEnglish
dc.publisherWILEY-BLACKWELL
dc.subjectNeurology and Neuromuscular Diseases; Autoimmunity; Medical Biochemistry: Proteins and Peptides (incl. Medical Proteomics); Nervous System and Disorders
dc.titleN-linked glycosylation modulates dimerization of protein disulfide isomerase family A member 2 (PDIA2)
dc.typeJournal Article
dc.identifier.doi10.1111/febs.12063
melbourne.peerreviewPeer Reviewed
melbourne.affiliationThe University of Melbourne
melbourne.affiliation.departmentCentre For Neuroscience Research
melbourne.source.titleThe Federation of European Biochemical Societies (FEBS) Journal
melbourne.source.volume280
melbourne.source.issue1
melbourne.source.pages233-243
melbourne.identifier.nhmrc454749
melbourne.publicationid195767
melbourne.elementsid357426
melbourne.contributor.authorATKIN, JULIE
melbourne.contributor.authorWALKER, ADAM
dc.identifier.eissn1742-4658
melbourne.identifier.fundernameidNHMRC, 454749
melbourne.fieldofresearch320905 Neurology and neuromuscular diseases
melbourne.fieldofresearch320403 Autoimmunity
melbourne.fieldofresearch320506 Medical biochemistry - proteins and peptides (incl. medical proteomics)
melbourne.seocode200199 Clinical health not elsewhere classified
melbourne.accessrightsThis item is currently not available from this repository


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