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  Conditional modulation of membrane protein expression in cultured cells mediated by prionprotein recognition

Karpuj, M. V., Gelibter-Niv, S., Tiran, A., Rambold, A., Tatzelt, J., Nunziante, M., et al. (2011). Conditional modulation of membrane protein expression in cultured cells mediated by prionprotein recognition. The Journal of Biological Chemistry, 286, 6911-6917. doi:10.1074/jbc.M110.194662.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-C4E6-A Version Permalink: http://hdl.handle.net/21.11116/0000-0007-A8AF-7
Genre: Journal Article

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https://www.jbc.org/content/286/9/6911.long (Publisher version)
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 Creators:
Karpuj, Marcela Viviana1, Author
Gelibter-Niv, Sagit1, Author
Tiran, Anat1, Author
Rambold, Angelika2, Author              
Tatzelt, Jörg1, Author
Nunziante, Max1, Author
Schatzl, Hermann M.1, Author
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1External Organizations, ou_persistent22              
2Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society, ou_2243650              

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 Abstract: We demonstrate that the levels of native as well as transfected prion protein (PrP) are lowered in various cell lines exposedto phosphorothioate oligodeoxynucleotides (PS-DNA) and can be rapidly reverted to their normal amounts by removal of PS-DNA.This transient modulation was independent of the glycosylation state of PrP, and in addition, all three PrP glycoforms weresusceptible to PS-DNA treatment. Deletion of the N-terminal domain (amino acids 23–99), but not of the other domains of PrP,abrogated its PS-DNA-mediated down-regulation. PrP versions localized in the mitochondria, cytoplasm, or nucleus were notmodulated by PS-DNA, indicating that PrP surface exposure is required for executing this effect. Proteins that in their nativeforms were not responsive to PS-DNA, such as thymocyte antigen 1 (Thy1), Doppel protein (Dpl), green fluorescent protein (GFP),and cyan fluorescent protein (CFP), became susceptible to PS-DNA-mediated down-regulation following introduction of the Nterminus of PrP into their sequence. These observations demonstrate the essential role of the N-terminal domain for promotingoligonucleotide-mediated reduction of the PrP level and suggest that transient treatment of cultured cells with PS-DNA mayprovide a general method for targeted modulation of the levels of desired surface proteins in a conditional and reversiblemanner.

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Language(s): eng - English
 Dates: 2011
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1074/jbc.M110.194662
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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 286 Sequence Number: - Start / End Page: 6911 - 6917 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1