Oxidative stress mislocalizes and retains transport factor importin-alpha and nucleoporins Nup153 and Nup88 in nuclei where they generate high molecular mass complexes - PubMed (original) (raw)
. 2008 Mar;1783(3):405-18.
doi: 10.1016/j.bbamcr.2007.10.022. Epub 2007 Nov 17.
Affiliations
- PMID: 18068677
- DOI: 10.1016/j.bbamcr.2007.10.022
Free article
Oxidative stress mislocalizes and retains transport factor importin-alpha and nucleoporins Nup153 and Nup88 in nuclei where they generate high molecular mass complexes
Mohamed Kodiha et al. Biochim Biophys Acta. 2008 Mar.
Free article
Abstract
Nuclear trafficking of proteins requires the cooperation between soluble transport components and nucleoporins. As such, classical nuclear import depends on the dimeric carrier importin-alpha/beta1, and CAS, a member of the importin-beta family, which exports importin-alpha to the cytoplasm. Here we analyzed the effect of oxidative stress elicited by diethyl maleate (DEM) on classical nuclear transport. Under conditions that do not induce death in the majority of cells, DEM has little effect on the nucleocytoplasmic concentration gradient of Ran, but interferes with the nuclear accumulation of several reporter proteins. Moreover, DEM treatment alters the distribution of soluble transport factors and several nucleoporins in growing cells. We identified nuclear retention of importin-alpha, CAS as well as nucleoporins Nup153 and Nup88 as a mechanism that contributes to the nuclear concentration of these proteins. Both nucleoporins, but not CAS, associate with importin-alpha in the nuclei of growing cells and in vitro. Importin-alpha generates high molecular mass complexes in the nucleus that contain Nup153 and Nup88, whereas CAS was not detected. The formation of high molecular mass complexes containing importin-alpha, Nup153 and Nup88 is increased upon oxidant treatment, suggesting that complex formation contributes to the anchoring of importin-alpha in nuclei. Taken together, our studies link oxidative stress to the proper localization of soluble transport factors and nucleoporins and to changes in the interactions between these proteins.
Similar articles
- Dissecting the signaling events that impact classical nuclear import and target nuclear transport factors.
Kodiha M, Tran D, Morogan A, Qian C, Stochaj U. Kodiha M, et al. PLoS One. 2009 Dec 24;4(12):e8420. doi: 10.1371/journal.pone.0008420. PLoS One. 2009. PMID: 20041180 Free PMC article. - Multiple mechanisms promote the inhibition of classical nuclear import upon exposure to severe oxidative stress.
Kodiha M, Chu A, Matusiewicz N, Stochaj U. Kodiha M, et al. Cell Death Differ. 2004 Aug;11(8):862-74. doi: 10.1038/sj.cdd.4401432. Cell Death Differ. 2004. PMID: 15088071 - The interaction between importin-α and Nup153 promotes importin-α/β-mediated nuclear import.
Ogawa Y, Miyamoto Y, Oka M, Yoneda Y. Ogawa Y, et al. Traffic. 2012 Jul;13(7):934-46. doi: 10.1111/j.1600-0854.2012.01367.x. Epub 2012 May 14. Traffic. 2012. PMID: 22510057 - Importin alpha: a multipurpose nuclear-transport receptor.
Goldfarb DS, Corbett AH, Mason DA, Harreman MT, Adam SA. Goldfarb DS, et al. Trends Cell Biol. 2004 Sep;14(9):505-14. doi: 10.1016/j.tcb.2004.07.016. Trends Cell Biol. 2004. PMID: 15350979 Review. - Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import.
Stewart M, Baker RP, Bayliss R, Clayton L, Grant RP, Littlewood T, Matsuura Y. Stewart M, et al. FEBS Lett. 2001 Jun 8;498(2-3):145-9. doi: 10.1016/s0014-5793(01)02489-9. FEBS Lett. 2001. PMID: 11412846 Review.
Cited by
- Altered Nup153 Expression Impairs the Function of Cultured Hippocampal Neural Stem Cells Isolated from a Mouse Model of Alzheimer's Disease.
Leone L, Colussi C, Gironi K, Longo V, Fusco S, Li Puma DD, D'Ascenzo M, Grassi C. Leone L, et al. Mol Neurobiol. 2019 Aug;56(8):5934-5949. doi: 10.1007/s12035-018-1466-1. Epub 2019 Jan 28. Mol Neurobiol. 2019. PMID: 30689197 - Dissecting the signaling events that impact classical nuclear import and target nuclear transport factors.
Kodiha M, Tran D, Morogan A, Qian C, Stochaj U. Kodiha M, et al. PLoS One. 2009 Dec 24;4(12):e8420. doi: 10.1371/journal.pone.0008420. PLoS One. 2009. PMID: 20041180 Free PMC article. - Regulation of nucleocytoplasmic transport in skeletal muscle.
Hall MN, Corbett AH, Pavlath GK. Hall MN, et al. Curr Top Dev Biol. 2011;96:273-302. doi: 10.1016/B978-0-12-385940-2.00010-3. Curr Top Dev Biol. 2011. PMID: 21621074 Free PMC article. Review. - Nucleoporin 88 (Nup88) is regulated by hypertonic stress in kidney cells to retain the transcription factor tonicity enhancer-binding protein (TonEBP) in the nucleus.
Andres-Hernando A, Lanaspa MA, Rivard CJ, Berl T. Andres-Hernando A, et al. J Biol Chem. 2008 Sep 5;283(36):25082-90. doi: 10.1074/jbc.M802381200. Epub 2008 Jul 7. J Biol Chem. 2008. PMID: 18606815 Free PMC article. - Data in support of 5'AMP-activated protein kinase alpha regulates stress granule biogenesis.
Mahboubi H, Barisé R, Stochaj U. Mahboubi H, et al. Data Brief. 2015 May 5;4:54-9. doi: 10.1016/j.dib.2015.04.010. eCollection 2015 Sep. Data Brief. 2015. PMID: 26217763 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Research Materials
Miscellaneous