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The NOXO1β PX domain preferentially targets PtdIns(4,5)P2 and PtdIns(3,4,5)P3.
- Source :
-
Journal of molecular biology [J Mol Biol] 2012 Apr 13; Vol. 417 (5), pp. 440-53. Date of Electronic Publication: 2012 Feb 08. - Publication Year :
- 2012
-
Abstract
- NOXO1β [NOXO1 (Nox organizer 1) β] is a cytosolic protein that, in conjunction with NOXA1 (Nox activator 1), regulates generation of reactive oxygen species by the NADPH oxidase 1 (Nox1) enzyme complex. NOXO1β is targeted to membranes through an N-terminal PX (phox homology) domain. We have used NMR spectroscopy to solve the structure of the NOXO1β PX domain and surface plasmon resonance (SPR) to assess phospholipid specificity. The solution structure of the NOXO1β PX domain shows greatest similarity to that of the phosphatidylinositol 3-kinase-C2α PX domain with regard to the positions and types of residues that are predicted to interact with phosphatidylinositol phosphate (PtdInsP) head groups. SPR experiments identify PtdIns(4,5)P(2) and PtdIns(3,4,5)P(3) as preferred targets of NOXO1β PX. These findings contrast with previous lipid overlay experiments showing strongest binding to monophosphorylated PtdInsP and phosphatidylserine. Our data suggest that localized membrane accumulation of PtdIns(4,5)P(2) or PtdIns(3,4,5)P(2) may serve to recruit NOXO1β and activate Nox1.<br /> (Copyright © 2012 Elsevier Ltd. All rights reserved.)
- Subjects :
- Adaptor Proteins, Signal Transducing
Amino Acid Sequence
Binding Sites
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Sequence Data
Protein Binding
Protein Conformation
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Surface Plasmon Resonance
Adaptor Proteins, Vesicular Transport chemistry
Adaptor Proteins, Vesicular Transport metabolism
Phosphatidylinositol 4,5-Diphosphate metabolism
Phosphatidylinositol Phosphates metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1089-8638
- Volume :
- 417
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Journal of molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 22342885
- Full Text :
- https://doi.org/10.1016/j.jmb.2012.01.058