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| | ==Structure of yeast importin a bound to the membrane protein Nuclear Localization Signal sequence of INM protein Heh2== | | ==Structure of yeast importin a bound to the membrane protein Nuclear Localization Signal sequence of INM protein Heh2== |
| - | <StructureSection load='4pvz' size='340' side='right' caption='[[4pvz]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='4pvz' size='340' side='right'caption='[[4pvz]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4pvz]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PVZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PVZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4pvz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PVZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PVZ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bk5|1bk5]], [[1ee4|1ee4]], [[1ee5|1ee5]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pvz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pvz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pvz RCSB], [http://www.ebi.ac.uk/pdbsum/4pvz PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4pvz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pvz OCA], [https://pdbe.org/4pvz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pvz RCSB], [https://www.ebi.ac.uk/pdbsum/4pvz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pvz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/IMA1_YEAST IMA1_YEAST]] Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope. Seems to act as a cytosolic receptor for both simple and bipartite NLS motifs (By similarity).<ref>PMID:7565597</ref> <ref>PMID:10913188</ref> <ref>PMID:21075847</ref> | + | [https://www.uniprot.org/uniprot/IMA1_YEAST IMA1_YEAST] Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope. Seems to act as a cytosolic receptor for both simple and bipartite NLS motifs (By similarity).<ref>PMID:7565597</ref> <ref>PMID:10913188</ref> <ref>PMID:21075847</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4pvz" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Importin 3D structures|Importin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bhardwaj, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Cingolani, C]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Hapsari, A R]] | + | [[Category: Bhardwaj A]] |
| - | [[Category: Lokareddy, R K]] | + | [[Category: Cingolani C]] |
| - | [[Category: Rheenen, M van]] | + | [[Category: Hapsari AR]] |
| - | [[Category: Veenhoff, L M]] | + | [[Category: Lokareddy RK]] |
| - | [[Category: Armadillo repeated structure]] | + | [[Category: Veenhoff LM]] |
| - | [[Category: Importin beta]] | + | [[Category: Van Rheenen M]] |
| - | [[Category: Nls-cargo]]
| + | |
| - | [[Category: Nuclear import adapter]]
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| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Function
IMA1_YEAST Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope. Seems to act as a cytosolic receptor for both simple and bipartite NLS motifs (By similarity).[1] [2] [3]
Publication Abstract from PubMed
Targeting of ER-synthesized membrane proteins to the inner nuclear membrane (INM) has long been explained by the diffusion-retention model. However, several INM proteins contain non-classical nuclear localization signal (NLS) sequences, which, in a few instances, have been shown to promote importin alpha/beta- and Ran-dependent translocation to the INM. Here, using structural and biochemical methods, we show that yeast INM proteins Heh2 and Src1/Heh1 contain bipartite import sequences that associate intimately with the minor NLS-binding pocket of yeast importin alpha and unlike classical NLSs efficiently displace the IBB domain in the absence of importin beta. In vivo, the intimate interactions at the minor NLS-binding pocket make the h2NLS highly efficient at recruiting importin alpha at the ER and drive INM localization of endogenous Heh2. Thus, h1/h2NLSs delineate a novel class of super-potent, IBB-like membrane protein NLSs, distinct from classical NLSs found in soluble cargos and of general interest in biology.
Distinctive Properties of the Nuclear Localization Signals of Inner Nuclear Membrane Proteins Heh1 and Heh2.,Lokareddy RK, Hapsari RA, van Rheenen M, Pumroy RA, Bhardwaj A, Steen A, Veenhoff LM, Cingolani G Structure. 2015 May 19. pii: S0969-2126(15)00175-6. doi:, 10.1016/j.str.2015.04.017. PMID:26051712[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kussel P, Frasch M. Yeast Srp1, a nuclear protein related to Drosophila and mouse pendulin, is required for normal migration, division, and integrity of nuclei during mitosis. Mol Gen Genet. 1995 Aug 21;248(3):351-63. PMID:7565597
- ↑ Tabb MM, Tongaonkar P, Vu L, Nomura M. Evidence for separable functions of Srp1p, the yeast homolog of importin alpha (Karyopherin alpha): role for Srp1p and Sts1p in protein degradation. Mol Cell Biol. 2000 Aug;20(16):6062-73. PMID:10913188
- ↑ Chen L, Romero L, Chuang SM, Tournier V, Joshi KK, Lee JA, Kovvali G, Madura K. Sts1 plays a key role in targeting proteasomes to the nucleus. J Biol Chem. 2011 Jan 28;286(4):3104-18. doi: 10.1074/jbc.M110.135863. Epub 2010 , Nov 12. PMID:21075847 doi:10.1074/jbc.M110.135863
- ↑ Lokareddy RK, Hapsari RA, van Rheenen M, Pumroy RA, Bhardwaj A, Steen A, Veenhoff LM, Cingolani G. Distinctive Properties of the Nuclear Localization Signals of Inner Nuclear Membrane Proteins Heh1 and Heh2. Structure. 2015 May 19. pii: S0969-2126(15)00175-6. doi:, 10.1016/j.str.2015.04.017. PMID:26051712 doi:http://dx.doi.org/10.1016/j.str.2015.04.017
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