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| | ==Solution structure of the capsid domain from the activity-regulated cytoskeleton-associated protein, Arc== | | ==Solution structure of the capsid domain from the activity-regulated cytoskeleton-associated protein, Arc== |
| - | <StructureSection load='6gse' size='340' side='right'caption='[[6gse]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='6gse' size='340' side='right'caption='[[6gse]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6gse]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GSE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GSE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6gse]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GSE FirstGlance]. <br> |
| - | </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=6gse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gse OCA], [http://pdbe.org/6gse PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gse RCSB], [http://www.ebi.ac.uk/pdbsum/6gse PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gse ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Hybrid , Solution NMR , X-ray solution scattering</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=6gse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gse OCA], [https://pdbe.org/6gse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gse RCSB], [https://www.ebi.ac.uk/pdbsum/6gse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gse ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ARC_RAT ARC_RAT]] Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the stress fiber dynamics and cell migration (By similarity). Required for consolidation of synaptic plasticity as well as formation of long-term memory. Regulates endocytosis of AMPA receptors in response to synaptic activity. Required for homeostatic synaptic scaling of AMPA receptors.<ref>PMID:17088212</ref> <ref>PMID:17088213</ref> | + | [https://www.uniprot.org/uniprot/ARC_RAT ARC_RAT] Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the stress fiber dynamics and cell migration (By similarity). Required for consolidation of synaptic plasticity as well as formation of long-term memory. Regulates endocytosis of AMPA receptors in response to synaptic activity. Required for homeostatic synaptic scaling of AMPA receptors.<ref>PMID:17088212</ref> <ref>PMID:17088213</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Erlendsson, S]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Nielsen, L D]] | + | [[Category: Erlendsson S]] |
| - | [[Category: Teilum, K]] | + | [[Category: Nielsen LD]] |
| - | [[Category: Gag protein]] | + | [[Category: Teilum K]] |
| - | [[Category: Nmda receptor interaction]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Retroviral capsid domain]]
| + | |
| Structural highlights
Function
ARC_RAT Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the stress fiber dynamics and cell migration (By similarity). Required for consolidation of synaptic plasticity as well as formation of long-term memory. Regulates endocytosis of AMPA receptors in response to synaptic activity. Required for homeostatic synaptic scaling of AMPA receptors.[1] [2]
Publication Abstract from PubMed
The activity-regulated cytoskeleton-associated protein, Arc, is highly expressed in neuronal dendrites and is involved in synaptic scaling and plasticity. Arc exhibits homology to the capsid-forming Gag proteins from retroviruses and can encapsulate its own mRNA and transport it to neighboring neurons. However, the molecular events that lead to the assembly of Arc capsids and how the capsid formation is regulated are not known. Here we show that the capsid domain of Arc may transiently form homogeneous oligomers of similar size as capsids formed by full-length Arc. We determined a high-resolution structure of the monomeric Arc capsid domain and mapped the initial structural change in the oligomerization process to the N-terminal part of the capsid domain. Peptide ligands from the NMDA receptor subunits inhibit oligomerization, which suggests that Arc's ability to transfer mRNA between cells may be regulated by protein-protein interactions at the synapse.
The Capsid Domain of Arc Changes Its Oligomerization Propensity through Direct Interaction with the NMDA Receptor.,Nielsen LD, Pedersen CP, Erlendsson S, Teilum K Structure. 2019 Apr 16. pii: S0969-2126(19)30123-6. doi:, 10.1016/j.str.2019.04.001. PMID:31080121[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rial Verde EM, Lee-Osbourne J, Worley PF, Malinow R, Cline HT. Increased expression of the immediate-early gene arc/arg3.1 reduces AMPA receptor-mediated synaptic transmission. Neuron. 2006 Nov 9;52(3):461-74. PMID:17088212 doi:http://dx.doi.org/10.1016/j.neuron.2006.09.031
- ↑ Shepherd JD, Rumbaugh G, Wu J, Chowdhury S, Plath N, Kuhl D, Huganir RL, Worley PF. Arc/Arg3.1 mediates homeostatic synaptic scaling of AMPA receptors. Neuron. 2006 Nov 9;52(3):475-84. PMID:17088213 doi:http://dx.doi.org/S0896-6273(06)00683-0
- ↑ Nielsen LD, Pedersen CP, Erlendsson S, Teilum K. The Capsid Domain of Arc Changes Its Oligomerization Propensity through Direct Interaction with the NMDA Receptor. Structure. 2019 Apr 16. pii: S0969-2126(19)30123-6. doi:, 10.1016/j.str.2019.04.001. PMID:31080121 doi:http://dx.doi.org/10.1016/j.str.2019.04.001
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