Importin: Difference between revisions
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**[[5huw]] – mIPO NLS-binding domain + HSVI large terminase<br /> | **[[5huw]] – mIPO NLS-binding domain + HSVI large terminase<br /> | ||
**[[5huy]] – mIPO NLS-binding domain + HSMV small terminase<br /> | **[[5huy]] – mIPO NLS-binding domain + HSMV small terminase<br /> | ||
**[[5hhg, [[5fc8]] – mIPO NLS-binding domain + dengue 2 NS5<br /> | **[[5hhg]], [[5fc8]] – mIPO NLS-binding domain + dengue 2 NS5<br /> | ||
**[[5ekg]], [[5ekf]], [[5e6q]] – mIPO NLS-binding domain + XPG2<br /> | **[[5ekg]], [[5ekf]], [[5e6q]] – mIPO NLS-binding domain + XPG2<br /> | ||
**[[5d5k]] – mIPO NLS-binding domain + PARP 2<br /> | **[[5d5k]] – mIPO NLS-binding domain + PARP 2<br /> |
Revision as of 12:43, 15 June 2017
FunctionImportins (IPO) mediate the import of cellular proteins into the nucleus by binding to the Nuclear Localization Signal (NLS). IPO has 2 subunits: α and β. IPO-α is an adaptor protein which binds the NLS[1]. IPOs can contain one or two NLS motifs. IPO-α contains several armadillo repeats with two NLS-binding sites and an IPO-β binding (IBB) site. IPO-β contains 19 HEAT (solenoid domain) repeats. Many nuclear proteins contain Phe-Gly sequences which can bind to HEAT repeats and thus be transported. See also Protein Transport Membrane Protein. DiseaseIPO-α isoform expression is altered in many kinds of cancer. RelevanceSpecific IPO-α isoforms are critical in nerve regenerative response after injury. Loss of IPO-α expression in aging myocardial cells could make recovery after heart disease in elderly patients more difficult[2]. Structural highlights |
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3D structures of importin3D structures of importin
Updated on 15-June-2017
ReferencesReferences
- ↑ Mattaj IW, Englmeier L. Nucleocytoplasmic transport: the soluble phase. Annu Rev Biochem. 1998;67:265-306. PMID:9759490 doi:http://dx.doi.org/10.1146/annurev.biochem.67.1.265
- ↑ Pumroy RA, Cingolani G. Diversification of importin-alpha isoforms in cellular trafficking and disease states. Biochem J. 2015 Feb 15;466(1):13-28. doi: 10.1042/BJ20141186. PMID:25656054 doi:http://dx.doi.org/10.1042/BJ20141186