D
IPR045808

FBXL5-like, hemerythrin-like domain

InterPro entry
Short nameHr_FBXL5
domain relationships

Description

Human FBXL5 (F-box and leucine-rich repeat protein 5) protein plays a role in cellular iron homeostasis
[2]
. It is part of an E3 ubiquitin ligase complex that targets the iron regulatory protein IRP2 for proteasomal degradation
[4]
. The FBXL5's stability is regulated by iron concentration, with its iron- and oxygen-binding hemerythrin domain acting as a ligand-dependent regulatory switch
[3, 1, 5]
.

References

1.Structural and molecular characterization of the iron-sensing hemerythrin-like domain within F-box and leucine-rich repeat protein 5 (FBXL5). Thompson JW, Salahudeen AA, Chollangi S, Ruiz JC, Brautigam CA, Makris TM, Lipscomb JD, Tomchick DR, Bruick RK. J. Biol. Chem. (2012). PMID: 22253436

2.An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis. Salahudeen AA, Thompson JW, Ruiz JC, Ma HW, Kinch LN, Li Q, Grishin NV, Bruick RK. Science 326, 722-6, (2009). View articlePMID: 19762597

3.The structural basis of iron sensing by the human F-box protein FBXL5. Shu C, Sung MW, Stewart MD, Igumenova TI, Tan X, Li P. Chembiochem 13, 788-91, (2012). View articlePMID: 22492618

4.Hemerythrin-like domain within F-box and leucine-rich repeat protein 5 (FBXL5) communicates cellular iron and oxygen availability by distinct mechanisms. Chollangi S, Thompson JW, Ruiz JC, Gardner KH, Bruick RK. J Biol Chem 287, 23710-7, (2012). PMID: 22648410

5.The FBXL5-IRP2 axis is integral to control of iron metabolism in vivo. Moroishi T, Nishiyama M, Takeda Y, Iwai K, Nakayama KI. Cell Metab 14, 339-51, (2011). PMID: 21907140

GO terms

molecular function

  • None

cellular component

  • None
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