7ykf: Difference between revisions
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==Crystal structure of MAGI2 PDZ0-GK/pEphexin4 complex== | |||
<StructureSection load='7ykf' size='340' side='right'caption='[[7ykf]], [[Resolution|resolution]] 2.28Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7ykf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YKF FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.28Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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=7ykf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ykf OCA], [https://pdbe.org/7ykf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ykf RCSB], [https://www.ebi.ac.uk/pdbsum/7ykf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ykf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MAGI2_MOUSE MAGI2_MOUSE] Seems to act as a scaffold molecule at synaptic junctions by assembling neurotransmitter receptors and cell adhesion proteins (By similarity). Plays a role in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and neurite outgrowth (By similarity). May play a role in regulating activin-mediated signaling in neuronal cells (PubMed:10681527). Enhances the ability of PTEN to suppress AKT1 activation (By similarity). Plays a role in receptor-mediated clathrin-dependent endocytosis which is required for ciliogenesis (PubMed:24608321).[UniProtKB:O88382][UniProtKB:Q86UL8]<ref>PMID:10681527</ref> <ref>PMID:24608321</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Dynamic signal transduction requires the rapid assembly and disassembly of signaling complexes, often mediated by phosphoprotein binding modules. The guanylate kinase-like (GK) domain of the membrane-associated guanylate kinases (MAGUKs) is such a module orchestrating signaling at cellular junctions. The MAGI subfamily of MAGUKs contains a truncated GK domain with unknown structure and function, although they participate in diverse physiological and pathological processes. Here, we demonstrate that the truncated GK domain of MAGI2 interacts with its adjacent PDZ0 domain to form a structural supramodule capable of recognizing phosphoproteins. A conserved phosphorylation-dependent binding motif for PDZ0-GK is delineated, which leads to identification of a set of previously unknown binding partners. We explore the structure and function of the MAGI2-target complex with an inhibitory peptide derived from the consensus motif. Our work reveals an action mechanism of the cryptic MAGI GKs and broadens our understanding of the target recognition rules of phosphoprotein binding modules. | |||
Phosphorylation-dependent recognition of diverse protein targets by the cryptic GK domain of MAGI MAGUKs.,Zhang M, Cao A, Lin L, Chen Y, Shang Y, Wang C, Zhang M, Zhu J Sci Adv. 2023 May 10;9(19):eadf3295. doi: 10.1126/sciadv.adf3295. Epub 2023 May , 10. PMID:37163606<ref>PMID:37163606</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7ykf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Lin L]] | |||
[[Category: Zhang M]] | |||
[[Category: Zhu J]] | |||
Latest revision as of 14:47, 23 October 2024
Crystal structure of MAGI2 PDZ0-GK/pEphexin4 complexCrystal structure of MAGI2 PDZ0-GK/pEphexin4 complex
Structural highlights
FunctionMAGI2_MOUSE Seems to act as a scaffold molecule at synaptic junctions by assembling neurotransmitter receptors and cell adhesion proteins (By similarity). Plays a role in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and neurite outgrowth (By similarity). May play a role in regulating activin-mediated signaling in neuronal cells (PubMed:10681527). Enhances the ability of PTEN to suppress AKT1 activation (By similarity). Plays a role in receptor-mediated clathrin-dependent endocytosis which is required for ciliogenesis (PubMed:24608321).[UniProtKB:O88382][UniProtKB:Q86UL8][1] [2] Publication Abstract from PubMedDynamic signal transduction requires the rapid assembly and disassembly of signaling complexes, often mediated by phosphoprotein binding modules. The guanylate kinase-like (GK) domain of the membrane-associated guanylate kinases (MAGUKs) is such a module orchestrating signaling at cellular junctions. The MAGI subfamily of MAGUKs contains a truncated GK domain with unknown structure and function, although they participate in diverse physiological and pathological processes. Here, we demonstrate that the truncated GK domain of MAGI2 interacts with its adjacent PDZ0 domain to form a structural supramodule capable of recognizing phosphoproteins. A conserved phosphorylation-dependent binding motif for PDZ0-GK is delineated, which leads to identification of a set of previously unknown binding partners. We explore the structure and function of the MAGI2-target complex with an inhibitory peptide derived from the consensus motif. Our work reveals an action mechanism of the cryptic MAGI GKs and broadens our understanding of the target recognition rules of phosphoprotein binding modules. Phosphorylation-dependent recognition of diverse protein targets by the cryptic GK domain of MAGI MAGUKs.,Zhang M, Cao A, Lin L, Chen Y, Shang Y, Wang C, Zhang M, Zhu J Sci Adv. 2023 May 10;9(19):eadf3295. doi: 10.1126/sciadv.adf3295. Epub 2023 May , 10. PMID:37163606[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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