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| <StructureSection load='5zz9' size='340' side='right'caption='[[5zz9]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='5zz9' size='340' side='right'caption='[[5zz9]], [[Resolution|resolution]] 2.30Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[5zz9]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZZ9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZZ9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5zz9]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZZ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZZ9 FirstGlance]. <br> |
- | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Homer2, Vesl2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), DBN1, D0S117E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 2.3Å</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5zz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zz9 OCA], [http://pdbe.org/5zz9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zz9 RCSB], [http://www.ebi.ac.uk/pdbsum/5zz9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zz9 ProSAT]</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=5zz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zz9 OCA], [https://pdbe.org/5zz9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zz9 RCSB], [https://www.ebi.ac.uk/pdbsum/5zz9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zz9 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/HOME2_MOUSE HOME2_MOUSE]] Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. May also couple GRM1 to PI3 kinase through its interaction with AGAP2. Isoforms can be differently regulated and may play an important role in maintaining the plasticity at glutamatergic synapses. [[http://www.uniprot.org/uniprot/DREB_HUMAN DREB_HUMAN]] Drebrins might play some role in cell migration, extension of neuronal processes and plasticity of dendrites. Required for actin polymerization at immunological synapses (IS) and for CXCR4 recruitment to IS.<ref>PMID:20215400</ref> | + | [https://www.uniprot.org/uniprot/HOME2_MOUSE HOME2_MOUSE] Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. May also couple GRM1 to PI3 kinase through its interaction with AGAP2. Isoforms can be differently regulated and may play an important role in maintaining the plasticity at glutamatergic synapses. |
| <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: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
- | [[Category: Li, J]] | + | [[Category: Li J]] |
- | [[Category: Li, Z]] | + | [[Category: Li Z]] |
- | [[Category: Liu, H]] | + | [[Category: Liu H]] |
- | [[Category: Liu, W]] | + | [[Category: Liu W]] |
- | [[Category: Zhang, M]] | + | [[Category: Zhang M]] |
- | [[Category: Polyproline recognition]]
| + | |
- | [[Category: Protein binding]]
| + | |
- | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
HOME2_MOUSE Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. May also couple GRM1 to PI3 kinase through its interaction with AGAP2. Isoforms can be differently regulated and may play an important role in maintaining the plasticity at glutamatergic synapses.
Publication Abstract from PubMed
Drebrin is an actin bundling protein that plays critical roles in synaptic spine development and plasticity. Homer, one of the most abundant scaffolding proteins in postsynaptic density, interacts with Drebrin's C-terminal PPXXF motifs using its Ena/VASP homology 1 (EVH1) domain. However, the molecular mechanism and biological function of this interaction remain unclear. Here we show that Homer specifically binds to the first but not the second PPXXF motif in Drebrin. The crystal structure of Drebrin-Homer binding motif 1 in complex with Homer EVH1 reveals a consensus Homer EVH1 binding motif. Homer tetramer promotes actin bundling activity of Drebrin in vitro and stimulates Drebrin-induced filopodia formation and elongation in cells. We further show that monomeric Homer1a antagonizes Homer1b in promoting Drebrin-stimulated actin bundling. Our study suggests a potential regulatory role of Homer1 in modulating excitatory synaptic spine homeostatic scaling via binding to Drebrin.
Homer Tetramer Promotes Actin Bundling Activity of Drebrin.,Li Z, Liu H, Li J, Yang Q, Feng Z, Li Y, Yang H, Yu C, Wan J, Liu W, Zhang M Structure. 2018 Nov 5. pii: S0969-2126(18)30372-1. doi:, 10.1016/j.str.2018.10.011. PMID:30503778[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li Z, Liu H, Li J, Yang Q, Feng Z, Li Y, Yang H, Yu C, Wan J, Liu W, Zhang M. Homer Tetramer Promotes Actin Bundling Activity of Drebrin. Structure. 2018 Nov 5. pii: S0969-2126(18)30372-1. doi:, 10.1016/j.str.2018.10.011. PMID:30503778 doi:http://dx.doi.org/10.1016/j.str.2018.10.011
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