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    FEBS Lett. 2001 Jun 1;498(1):62-6.

    Binding and regulation of HIF-1alpha by a subunit of the proteasome complex, PSMA7.

    Cho S, Choi YJ, Kim JM, Jeong ST, Kim JH, Kim SH, Ryu SE.

    Source

    Center for Cellular Switch Protein Structure, Korea Research Institute of Bioscience and Biotechnology, Yusong, Taejon, South Korea. scho@mail.kribb.re.kr

    Abstract

    The hypoxia-inducible factor-1alpha (HIF-1alpha) is an important transcription factor for cellular responses to oxygen tension. It is rapidly degraded under normoxic conditions by the ubiquitin-dependent proteasome pathway. Here we report a critical role of the 20S proteasome subunit PSMA7 in HIF-1alpha regulation. PSMA7 was found to interact specifically with two subdomains of HIF-1alpha. PSMA7 inhibited the transactivation function of HIF-1alpha under both normoxic and hypoxia-mimicking conditions. In addition, we show that the PSMA7-mediated regulation of HIF-1alpha activity is associated with the proteasome pathway.

    PMID:
    11389899
    [PubMed - indexed for MEDLINE]

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