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

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

  • FEBS Lett. 2001 Jun 1;498(1):62-6. doi: 10.1016/s0014-5793(01)02499-1.
S Cho 1,  Y J Choi,  J M Kim,  S T Jeong,  J H Kim,  S H Kim,  S E Ryu
Affiliations

Affiliation

  • 1 Center for Cellular Switch Protein Structure, Korea Research Institute of Bioscience and Biotechnology, Yusong, Taejon, South Korea. scho@mail.kribb.re.kr
PMID: 11389899 DOI: 10.1016/s0014-5793(01)02499-1
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.

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