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| | ==X-ray structure of human RBPMS== | | ==X-ray structure of human RBPMS== |
| - | <StructureSection load='5cyj' size='340' side='right' caption='[[5cyj]], [[Resolution|resolution]] 1.79Å' scene=''> | + | <StructureSection load='5cyj' size='340' side='right'caption='[[5cyj]], [[Resolution|resolution]] 1.79Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5cyj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CYJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CYJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5cyj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CYJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CYJ FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RBPMS, HERMES ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5cyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cyj OCA], [https://pdbe.org/5cyj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cyj RCSB], [https://www.ebi.ac.uk/pdbsum/5cyj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cyj ProSAT]</span></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=5cyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cyj OCA], [http://pdbe.org/5cyj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cyj RCSB], [http://www.ebi.ac.uk/pdbsum/5cyj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cyj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RBPMS_HUMAN RBPMS_HUMAN]] Acts as a coactivator of transcriptional activity. Required to increase TGFB1/Smad-mediated transactivation. Acts through SMAD2, SMAD3 and SMAD4 to increase transcriptional activity. Increases phosphorylation of SMAD2 and SMAD3 on their C-terminal SSXS motif, possibly through recruitment of TGFBR1. Promotes the nuclear accumulation of SMAD2, SMAD3 and SMAD4 proteins. Binds to poly(A) RNA.<ref>PMID:17099224</ref> | + | [https://www.uniprot.org/uniprot/RBPMS_HUMAN RBPMS_HUMAN] Acts as a coactivator of transcriptional activity. Required to increase TGFB1/Smad-mediated transactivation. Acts through SMAD2, SMAD3 and SMAD4 to increase transcriptional activity. Increases phosphorylation of SMAD2 and SMAD3 on their C-terminal SSXS motif, possibly through recruitment of TGFBR1. Promotes the nuclear accumulation of SMAD2, SMAD3 and SMAD4 proteins. Binds to poly(A) RNA.<ref>PMID:17099224</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Farazi, T A]] | + | [[Category: Large Structures]] |
| - | [[Category: Patel, D J]] | + | [[Category: Farazi TA]] |
| - | [[Category: Teplova, M]] | + | [[Category: Patel DJ]] |
| - | [[Category: Rna binding protein]] | + | [[Category: Teplova M]] |
| - | [[Category: Rna-binding protein]]
| + | |
| - | [[Category: Rrm domain]]
| + | |
| Structural highlights
Function
RBPMS_HUMAN Acts as a coactivator of transcriptional activity. Required to increase TGFB1/Smad-mediated transactivation. Acts through SMAD2, SMAD3 and SMAD4 to increase transcriptional activity. Increases phosphorylation of SMAD2 and SMAD3 on their C-terminal SSXS motif, possibly through recruitment of TGFBR1. Promotes the nuclear accumulation of SMAD2, SMAD3 and SMAD4 proteins. Binds to poly(A) RNA.[1]
Publication Abstract from PubMed
RNA-binding protein with multiple splicing (designated RBPMS) is a higher vertebrate mRNA-binding protein containing a single RNA recognition motif (RRM). RBPMS has been shown to be involved in mRNA transport, localization and stability, with key roles in axon guidance, smooth muscle plasticity, as well as regulation of cancer cell proliferation and migration. We report on structure-function studies of the RRM domain of RBPMS bound to a CAC-containing single-stranded RNA. These results provide insights into potential topologies of complexes formed by the RBPMS RRM domain and the tandem CAC repeat binding sites as detected by photoactivatable-ribonucleoside-enhanced crosslinking and immunoprecipitation. These studies establish that the RRM domain of RBPMS forms a symmetrical dimer in the free state, with each monomer binding sequence-specifically to all three nucleotides of a CAC segment in the RNA bound state. Structure-guided mutations within the dimerization and RNA-binding interfaces of RBPMS RRM on RNA complex formation resulted in both disruption of dimerization and a decrease in RNA-binding affinity as observed by size exclusion chromatography and isothermal titration calorimetry. As anticipated from biochemical binding studies, over-expression of dimerization or RNA-binding mutants of Flag-HA-tagged RBPMS were no longer able to track with stress granules in HEK293 cells, thereby documenting the deleterious effects of such mutations in vivo.
Structural basis underlying CAC RNA recognition by the RRM domain of dimeric RNA-binding protein RBPMS.,Teplova M, Farazi TA, Tuschl T, Patel DJ Q Rev Biophys. 2015 Sep 8:1-11. PMID:26347403[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sun Y, Ding L, Zhang H, Han J, Yang X, Yan J, Zhu Y, Li J, Song H, Ye Q. Potentiation of Smad-mediated transcriptional activation by the RNA-binding protein RBPMS. Nucleic Acids Res. 2006;34(21):6314-26. Epub 2006 Nov 11. PMID:17099224 doi:http://dx.doi.org/10.1093/nar/gkl914
- ↑ Teplova M, Farazi TA, Tuschl T, Patel DJ. Structural basis underlying CAC RNA recognition by the RRM domain of dimeric RNA-binding protein RBPMS. Q Rev Biophys. 2015 Sep 8:1-11. PMID:26347403 doi:http://dx.doi.org/10.1017/S0033583515000207
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