Hip2 interacts with cyclin B1 and promotes its degradation through the ubiquitin proteasome pathway

  • Yoonhee Bae
  • , Dongwon Choi
  • , Hyangshuk Rhim
  • , Seongman Kang*
  • *Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    13 Citations (Scopus)

    Abstract

    Hip2, a ubiquitin conjugating enzyme, is involved in the suppression of cell death. The present study revealed that Hip2 regulates the stability of the apoptotic and cell cycle regulator cyclin B1. Hip2 was found to interact with cyclin B1 to promote its degradation through the ubiquitin proteasome pathway. As a result, Hip2 significantly blocked cell death induced by the cyclin B1 protein, suggesting that Hip2 is involved in the regulation of cyclin B1-mediated cell death. Structured summary: MINT- 8045218, MINT- 8045231: Hip2 (uniprotkb: P61086) physically interacts (MI: 0915) with cyclin-B1 (uniprotkb: P14635) by pull down (MI: 0096).

    Original languageEnglish
    Pages (from-to)4505-4510
    Number of pages6
    JournalFEBS Letters
    Volume584
    Issue number22
    DOIs
    Publication statusPublished - 2010 Nov 19

    Bibliographical note

    Funding Information:
    This work was supported by the National Research Foundation of Korea (NRF) Grant funded by the Korea government ( 200601742 ) and a Grant from the Korea Healthcare Technology R&D Project, Ministry for Health, Welfare & Family Affairs , the Republic of Korea ( A084358 ). Also, we are thank Ok Jeong Noh and Juno Jang for helpful material and method.

    Keywords

    • Apoptosis
    • Cyclin B1
    • Hip2
    • Ubiquitination

    ASJC Scopus subject areas

    • Biophysics
    • Structural Biology
    • Biochemistry
    • Molecular Biology
    • Genetics
    • Cell Biology

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