liu.seSearch for publications in DiVA
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Interaction with PI3-kinase contributes to the cytotoxic activity of Apoptin
Department of Biochemistry and Medical Genetics, University of Manitoba, Winnipeg, Manitoba, Canada; Manitoba Institute of Cell Biology, CancerCare Manitoba, University of Manitoba, Winnipeg, Manitoba, Canada; Department of Therapeutic Radiology, Yale School of Medicine, New Haven, USA.
Manitoba Institute of Cell Biology, CancerCare Manitoba; Department of Human Genetics, University of Aarhus, Aarhus, Denmark,.
Department of Biochemistry and Medical Genetics, University of Manitoba, Winnipeg, Manitoba, Canada; Manitoba Institute of Cell Biology, CancerCare Manitoba, University of Manitoba, Winnipeg, Manitoba, Canada.
Nuclear Signaling Laboratory, Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria, Australia.
Show others and affiliations
2008 (English)In: Oncogene, ISSN 0950-9232, E-ISSN 1476-5594, Vol. 27, 3060-3065 p.Article in journal (Refereed) Published
Abstract [en]

Apoptin, a small protein from the chicken anemia virus, has attracted attention because of its specificity in killing tumor cells. Localization of apoptin in the nucleus of tumor cells has been shown to be vital for proapoptotic activity, however, targeted expression of apoptin in the nucleus of normal cells does not harm the cells, indicating that nuclear localization of apoptin is insufficient for its cytotoxicity. Here, we demonstrate for the first time that apoptin interacts with the SH3 domain of p85, the regulatory subunit of phosphoinositide 3-kinase (PI3-K), through its proline-rich region. Apoptin derivatives devoid of this proline-rich region do not interact with p85, are unable to activate PI3-K, and show impaired apoptosis induction. Moreover, apoptin mutants containing the proline-rich domain are sufficient to elevate PI3-K activity and to induce apoptosis in cancer cells. Downregulation of p85 leads to nuclear exclusion of apoptin and impairs cell death induction, indicating that interaction with the p85 PI3-K subunit essentially contributes to the cytotoxic activity of apoptin.

Place, publisher, year, edition, pages
Nature Publishing Group, 2008. Vol. 27, 3060-3065 p.
Keyword [en]
anticancer drugs, apoptin, apoptosis, PI3-kinase
National Category
Cancer and Oncology Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy) Biochemistry and Molecular Biology Cell Biology
Identifiers
URN: urn:nbn:se:liu:diva-86928DOI: 10.1038/sj.onc.1210958ISI: 000255681700013PubMedID: 18059340OAI: oai:DiVA.org:liu-86928DiVA: diva2:583315
Available from: 2013-01-07 Created: 2013-01-07 Last updated: 2017-12-06

Open Access in DiVA

fulltext(191 kB)109 downloads
File information
File name FULLTEXT01.pdfFile size 191 kBChecksum SHA-512
72009eba6b981d7ea7294d188e557cf5f38bda86a56e1a5c3baebe5c9bee31ea6dbdbccfeef83c9b185656f939068aa78fa4111ebb21a6597bc9facff1a8b7dd
Type fulltextMimetype application/pdf

Other links

Publisher's full textPubMed

Authority records BETA

Wiechec, EmiliaLos, Marek Jan

Search in DiVA

By author/editor
Wiechec, EmiliaLos, Marek Jan
In the same journal
Oncogene
Cancer and OncologyMedical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)Biochemistry and Molecular BiologyCell Biology

Search outside of DiVA

GoogleGoogle Scholar
Total: 109 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 330 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf