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Control of Iron Hom...
Control of Iron Homeostasis by an Iron-Regulated Ubiquitin Ligase
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Vashisht, Ajay A. (author)
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Zumbrennen, Kimberly B. (author)
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Huang, Xinhua (author)
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Powers, David N. (author)
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Durazo, Armando (author)
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Sun, Dahui (author)
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- Bhaskaran, Nimesh (author)
- Karolinska Institutet
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- Persson, Anja (author)
- KTH,Proteomik
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- Uhlén, Mathias (author)
- KTH,Proteomik
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- Sangfelt, Olle (author)
- Karolinska Institutet
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Spruck, Charles (author)
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Leibold, Elizabeth A. (author)
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Wohlschlegel, James A. (author)
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(creator_code:org_t)
- American Association for the Advancement of Science (AAAS), 2009
- 2009
- English.
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In: Science. - : American Association for the Advancement of Science (AAAS). - 0036-8075 .- 1095-9203. ; 326:5953, s. 718-721
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https://europepmc.or...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Subject headings
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- Eukaryotic cells require iron for survival and have developed regulatory mechanisms for maintaining appropriate intracellular iron concentrations. The degradation of iron regulatory protein 2 (IRP2) in iron-replete cells is a key event in this pathway, but the E3 ubiquitin ligase responsible for its proteolysis has remained elusive. We found that a SKP1-CUL1-FBXL5 ubiquitin ligase protein complex associates with and promotes the iron-dependent ubiquitination and degradation of IRP2. The F-box substrate adaptor protein FBXL5 was degraded upon iron and oxygen depletion in a process that required an iron-binding hemerythrin-like domain in its N terminus. Thus, iron homeostasis is regulated by a proteolytic pathway that couples IRP2 degradation to intracellular iron levels through the stability and activity of FBXL5.
Keyword
- protein identification technology
- element-binding protein
- degradation
- irp2
- proteasome
- pathway
- oxygen
Publication and Content Type
- ref (subject category)
- art (subject category)
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- By the author/editor
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Vashisht, Ajay A ...
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Zumbrennen, Kimb ...
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Huang, Xinhua
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Powers, David N.
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Durazo, Armando
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Sun, Dahui
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show more...
-
Bhaskaran, Nimes ...
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Persson, Anja
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Uhlén, Mathias
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Sangfelt, Olle
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Spruck, Charles
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Leibold, Elizabe ...
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Wohlschlegel, Ja ...
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Science
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Royal Institute of Technology
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Karolinska Institutet