Show simple item record

Nuclear localization of Hif‐3α requires two redundant NLS motifs in its unique C‐terminal region

dc.contributor.authorYao, Qing
dc.contributor.authorZhang, Peng
dc.contributor.authorLu, Ling
dc.contributor.authorLiu, Yunzhang
dc.contributor.authorLi, Yun
dc.contributor.authorDuan, Cunming
dc.date.accessioned2018-09-04T20:09:12Z
dc.date.available2019-09-04T20:15:39Zen
dc.date.issued2018-08
dc.identifier.citationYao, Qing; Zhang, Peng; Lu, Ling; Liu, Yunzhang; Li, Yun; Duan, Cunming (2018). "Nuclear localization of Hif‐3α requires two redundant NLS motifs in its unique C‐terminal region." FEBS Letters 592(16): 2769-2775.
dc.identifier.issn0014-5793
dc.identifier.issn1873-3468
dc.identifier.urihttps://hdl.handle.net/2027.42/145561
dc.publisherWiley Periodicals, Inc.
dc.subject.otherzebrafish
dc.subject.otherhypoxia
dc.subject.otherhypoxia‐inducible factor
dc.subject.othernuclear localization signal
dc.titleNuclear localization of Hif‐3α requires two redundant NLS motifs in its unique C‐terminal region
dc.typeArticleen_US
dc.rights.robotsIndexNoFollow
dc.subject.hlbsecondlevelBiological Chemistry
dc.subject.hlbtoplevelScience
dc.description.peerreviewedPeer Reviewed
dc.description.bitstreamurlhttps://deepblue.lib.umich.edu/bitstream/2027.42/145561/1/feb213202_am.pdf
dc.description.bitstreamurlhttps://deepblue.lib.umich.edu/bitstream/2027.42/145561/2/feb213202.pdf
dc.identifier.doi10.1002/1873-3468.13202
dc.identifier.sourceFEBS Letters
dc.identifier.citedreferenceTazuke SI, Mazure NM, Sugawara J, Carland G, Faessen GH, Suen LF, Irwin JC, Powell DR, Giaccia AJ and Giudice LC ( 1998 ) Hypoxia stimulates insulin‐like growth factor binding protein 1 (IGFBP‐1) gene expression in HepG2 cells: a possible model for IGFBP‐1 expression in fetal hypoxia. Proc Natl Acad Sci USA 95, 10188 – 10193.
dc.identifier.citedreferenceSemenza GL ( 2012 ) Hypoxia‐inducible factors in physiology and medicine. Cell 148, 399 – 408.
dc.identifier.citedreferenceKeith B, Johnson RS and Simon MC ( 2011 ) HIF1α and HIF2α: sibling rivalry in hypoxic tumor growth and progression. Nat Rev Cancer 12, 9 – 22.
dc.identifier.citedreferencePrabhakar NR and Semenza GL ( 2012 ) Adaptive and maladaptive cardiorespiratory responses to continuous and intermittent hypoxia mediated by hypoxia‐inducible factors 1 and 2. Physiol Rev 92, 967 – 1003.
dc.identifier.citedreferenceDuan C ( 2016 ) Hypoxia‐inducible factor 3 biology: complexities and emerging themes. Am J Physiol Cell Physiol 310, C260 – C269.
dc.identifier.citedreferenceKallio PJ, Okamoto K, O’Brien S, Carrero P, Makino Y, Tanaka H and Poellinger L ( 1998 ) Signal transduction in hypoxic cells: inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia‐inducible factor‐1alpha. EMBO J 17, 6573 – 6586.
dc.identifier.citedreferenceLuo JC and Shibuya M ( 2001 ) A variant of nuclear localization signal of bipartite‐type is required for the nuclear translocation of hypoxia inducible factors (1alpha, 2alpha and 3alpha). Oncogene 20, 1435 – 1444.
dc.identifier.citedreferenceZhang P, Yao Q, Lu L, Zhou J, Li Y, Liu Y and Duan C ( 2012 ) Molecular, functional, and gene expression analysis of zebrafish hypoxia‐inducible factor‐3α. Am J Physiol 303, R1165 – R1174.
dc.identifier.citedreferenceGu YZ, Moran SM, Hogenesch JB, Wartman L and Bradfield CA ( 1998 ) Molecular characterization and chromosomal localization of a third alpha‐class hypoxia inducible factor subunit, HIF3alpha. Gene Expr 7, 205 – 213.
dc.identifier.citedreferenceMakino Y, Cao R, Svensson K, Bertilsson G, Asman M, Tanaka H, Cao Y, Berkenstam A and Poellinger L ( 2001 ) Inhibitory PAS domain protein is a negative regulator of hypoxia‐inducible gene expression. Nature 414, 550 – 554.
dc.identifier.citedreferenceMakino Y, Uenishi R, Okamoto K, Isoe T, Hosono O, Tanaka H, Kanopka A, Poellinger L, Haneda M and Morimoto C ( 2007 ) Transcriptional up‐regulation of inhibitory PAS domain protein gene expression by hypoxia‐inducible factor 1 (HIF‐1): a negative feedback regulatory circuit in HIF‐1‐mediated signaling in hypoxic cells. J Biol Chem 282, 14073 – 14082.
dc.identifier.citedreferenceHara S, Hamada J, Kobayashi C, Kondo Y and Imura N ( 2001 ) Expression and characterization of hypoxia‐inducible factor (HIF)‐3alpha in human kidney: suppression of HIF‐mediated gene expression by HIF‐3alpha. Biochem Biophys Res Commun 287, 808 – 813.
dc.identifier.citedreferencePasanen A, Heikkila M, Rautavuoma K, Hirsila M, Kivirikko KI and Myllyharju J ( 2010 ) Hypoxia‐inducible factor (HIF)‐3a is subject to extensive alternative splicing in human tissues and cancer cells and is regulated by HIF‐1 but not HIF‐2. Int J Biochem Cell Biol 42, 1189 – 1200.
dc.identifier.citedreferenceZhang P, Yao Q, Lu L, Li Y and Duan C ( 2014 ) Hypoxia inducible factor‐3 is an oxygen‐dependent transcription activator and regulates a distinct transcriptional response to hypoxia. Cell Rep 6, 1110 – 1121.
dc.identifier.citedreferenceZhang P, Bai Y, Lu L, Li Y and Duan C ( 2016 ) An oxygen‐insensitive Hif‐3α isoform inhibits Wnt signaling by destabilizing the nuclear β‐catenin complex. eLife 5, pii: e08996.
dc.identifier.citedreferenceGrünwald D and Singer RH ( 2012 ) Multiscale dynamics in nucleocytoplasmic transport. Curr Opin Cell Biol 24, 100 – 106.
dc.identifier.citedreferenceBear J, Tan W, Zolotukhin AS, Tabernero C, Hudson EA and Felber BK ( 1999 ) Identification of novel import and export signals of human TAP, the protein that binds to the constitutive transport element of the type D retrovirus mRNAs. Mol Cell Biol 19, 6306 – 6317.
dc.identifier.citedreferenceMaynard MA, Evans AJ, Hosomi T, Hara S, Jewett MA and Ohh M ( 2005 ) Human HIF‐3alpha4 is a dominant‐negative regulator of HIF‐1 and is down‐regulated in renal cell carcinoma. FASEB J 19, 1396 – 1406.
dc.identifier.citedreferenceMaynard MA, Evans AJ, Shi W, Kim WY, Liu FF and Ohh M ( 2007 ) Dominant‐negative HIF‐3 alpha 4 suppresses VHL‐null renal cell carcinoma progression. Cell Cycle 6, 2810 – 2816.
dc.identifier.citedreferenceTorii S, Sakaki K, Otomo M, Saka K, Yasumoto K and Sogawa K ( 2013 ) Nucleocytoplasmic shuttling of IPAS by its unique nuclear import and export signals unshared with other HIF‐3α splice variants. J Biochem 154, 561 – 567.
dc.owningcollnameInterdisciplinary and Peer-Reviewed


Files in this item

Show simple item record

Remediation of Harmful Language

The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.

Accessibility

If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.