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Article: PRL-3 mediates the protein maturation of ULBP2 by regulating the tyrosine phosphorylation of HSP60

TitlePRL-3 mediates the protein maturation of ULBP2 by regulating the tyrosine phosphorylation of HSP60
Authors
Issue Date2015
Citation
Journal of Immunology, 2015, v. 194, n. 6, p. 2930-2941 How to Cite?
AbstractCopyright © 2015 by The American Association of Immunologists, Inc. Many malignant cells release the NKG2D ligand ULBP2 from their cell surface to evade immunosurveillance by NK cells and CD8 T cells. Although the shedding mechanism remains unclear, various inhibitors of matrix metalloproteinases have been shown to efficiently block the release of soluble ULBP2. The clinical use of these inhibitors, however, is limited because of adverse side effects. Using high-throughput screening technique, we identified a specific inhibitor of phosphatase of regenerating liver 3 (PRL-3) that could reduce the level of soluble ULBP2 in the culture supernatant of various cancer cell lines. Inhibition or gene knockdown of PRL-3 did not reduce ULBP2 shedding, but rather suppressed posttranslational maturation of ULBP2, resulting in intracellular retention of immature ULBP2.We then found that ULBP2 was constitutively associated with heat shock protein HSP60. Complete maturation of ULBP2 required tyrosine phosphorylation of HSP60 which was mediated by PRL-3.
Persistent Identifierhttp://hdl.handle.net/10722/294384
ISSN
2023 Impact Factor: 3.6
2023 SCImago Journal Rankings: 1.558
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLeung, Wai Hang-
dc.contributor.authorVong, Queenie P.-
dc.contributor.authorLin, Wenwei-
dc.contributor.authorBouck, David-
dc.contributor.authorWendt, Susanne-
dc.contributor.authorSullivan, Erin-
dc.contributor.authorLi, Ying-
dc.contributor.authorBari, Rafijul-
dc.contributor.authorChen, Taosheng-
dc.contributor.authorLeung, Wing-
dc.date.accessioned2020-12-03T08:22:36Z-
dc.date.available2020-12-03T08:22:36Z-
dc.date.issued2015-
dc.identifier.citationJournal of Immunology, 2015, v. 194, n. 6, p. 2930-2941-
dc.identifier.issn0022-1767-
dc.identifier.urihttp://hdl.handle.net/10722/294384-
dc.description.abstractCopyright © 2015 by The American Association of Immunologists, Inc. Many malignant cells release the NKG2D ligand ULBP2 from their cell surface to evade immunosurveillance by NK cells and CD8 T cells. Although the shedding mechanism remains unclear, various inhibitors of matrix metalloproteinases have been shown to efficiently block the release of soluble ULBP2. The clinical use of these inhibitors, however, is limited because of adverse side effects. Using high-throughput screening technique, we identified a specific inhibitor of phosphatase of regenerating liver 3 (PRL-3) that could reduce the level of soluble ULBP2 in the culture supernatant of various cancer cell lines. Inhibition or gene knockdown of PRL-3 did not reduce ULBP2 shedding, but rather suppressed posttranslational maturation of ULBP2, resulting in intracellular retention of immature ULBP2.We then found that ULBP2 was constitutively associated with heat shock protein HSP60. Complete maturation of ULBP2 required tyrosine phosphorylation of HSP60 which was mediated by PRL-3.-
dc.languageeng-
dc.relation.ispartofJournal of Immunology-
dc.titlePRL-3 mediates the protein maturation of ULBP2 by regulating the tyrosine phosphorylation of HSP60-
dc.typeArticle-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.4049/jimmunol.1400817-
dc.identifier.pmid25687758-
dc.identifier.pmcidPMC4355089-
dc.identifier.scopuseid_2-s2.0-84924560272-
dc.identifier.volume194-
dc.identifier.issue6-
dc.identifier.spage2930-
dc.identifier.epage2941-
dc.identifier.eissn1550-6606-
dc.identifier.isiWOS:000350755200053-
dc.identifier.issnl0022-1767-

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