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| | <StructureSection load='4z88' size='340' side='right'caption='[[4z88]], [[Resolution|resolution]] 2.09Å' scene=''> | | <StructureSection load='4z88' size='340' side='right'caption='[[4z88]], [[Resolution|resolution]] 2.09Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4z88]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z88 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z88 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4z88]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z88 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z88 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=4z88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z88 OCA], [https://pdbe.org/4z88 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z88 RCSB], [https://www.ebi.ac.uk/pdbsum/4z88 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z88 ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2csq|2csq]]</td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rbp, Dmel_CG43073 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=4z88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z88 OCA], [http://pdbe.org/4z88 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z88 RCSB], [http://www.ebi.ac.uk/pdbsum/4z88 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4z88 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/JIP1_DROME JIP1_DROME]] The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins (By similarity). | + | [https://www.uniprot.org/uniprot/A0A0B4JDC9_DROME A0A0B4JDC9_DROME] |
| | <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: Drome]] | + | [[Category: Drosophila melanogaster]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Boehme, M A]] | + | [[Category: Boehme MA]] |
| - | [[Category: Driller, J H]] | + | [[Category: Driller JH]] |
| - | [[Category: Holton, N]] | + | [[Category: Holton N]] |
| - | [[Category: Loll, B]] | + | [[Category: Loll B]] |
| - | [[Category: Siebert, M]] | + | [[Category: Siebert M]] |
| - | [[Category: Sigrist, S J]] | + | [[Category: Sigrist SJ]] |
| - | [[Category: Wahl, M C]] | + | [[Category: Wahl MC]] |
| - | [[Category: Active zone]]
| + | |
| - | [[Category: Aplip1]]
| + | |
| - | [[Category: Rim-binding protein]]
| + | |
| - | [[Category: Sh3 domain]]
| + | |
| - | [[Category: Synapse]]
| + | |
| Structural highlights
Function
A0A0B4JDC9_DROME
Publication Abstract from PubMed
Synaptic vesicles (SVs) fuse at active zones (AZs) covered by a protein scaffold, at Drosophila synapses comprised of ELKS family member Bruchpilot (BRP) and RIM-binding protein (RBP). We here demonstrate axonal co-transport of BRP and RBP using intravital live imaging, with both proteins co-accumulating in axonal aggregates of several transport mutants. RBP, via its C-terminal Src-homology 3 (SH3) domains, binds Aplip1/JIP1, a transport adaptor involved in kinesin-dependent SV transport. We show in atomic detail that RBP C-terminal SH3 domains bind a proline-rich (PxxP) motif of Aplip1/JIP1 with submicromolar affinity. Pointmutating this PxxP motif provoked formation of ectopic AZ-like structures at axonal membranes. Direct interactions between AZ proteins and transport adaptors seem to provide complex avidity and shield synaptic interaction surfaces of pre-assembled scaffold protein transport complexes, thus, favouring physiological synaptic AZ assembly over premature assembly at axonal membranes.
A high affinity RIM-binding protein/Aplip1 interaction prevents the formation of ectopic axonal active zones.,Siebert M, Bohme MA, Driller JH, Babikir H, Mampell MM, Rey U, Ramesh N, Matkovic T, Holton N, Reddy-Alla S, Gottfert F, Kamin D, Quentin C, Klinedinst S, Andlauer TF, Hell SW, Collins CA, Wahl MC, Loll B, Sigrist SJ Elife. 2015 Aug 14;4. doi: 10.7554/eLife.06935. PMID:26274777[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Siebert M, Bohme MA, Driller JH, Babikir H, Mampell MM, Rey U, Ramesh N, Matkovic T, Holton N, Reddy-Alla S, Gottfert F, Kamin D, Quentin C, Klinedinst S, Andlauer TF, Hell SW, Collins CA, Wahl MC, Loll B, Sigrist SJ. A high affinity RIM-binding protein/Aplip1 interaction prevents the formation of ectopic axonal active zones. Elife. 2015 Aug 14;4. doi: 10.7554/eLife.06935. PMID:26274777 doi:http://dx.doi.org/10.7554/eLife.06935
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