3wp1: Difference between revisions

Latest revision as of 06:18, 17 October 2024

Phosphorylation-dependent interaction between tumor suppressors Dlg and Lgl

Structural highlights

3wp1 is a 2 chain structure with sequence from Homo sapiens and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.804Å
Ligands:	SEP, SO4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DLG4_RAT Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B.^[1] ^[2]

Publication Abstract from PubMed

The tumor suppressors Discs Large (Dlg), Lethal giant larvae (Lgl) and Scribble are essential for the establishment and maintenance of epithelial cell polarity in metazoan. Dlg, Lgl and Scribble are known to interact strongly with each other genetically and form the evolutionarily conserved Scribble complex. Despite more than a decade of extensive research, it has not been demonstrated whether Dlg, Lgl and Scribble physically interact with each other. Here, we show that Dlg directly interacts with Lgl in a phosphorylation-dependent manner. Phosphorylation of any one of the three conserved Ser residues situated in the central linker region of Lgl is sufficient for its binding to the Dlg guanylate kinase (GK) domain. The crystal structures of the Dlg4 GK domain in complex with two phosphor-Lgl2 peptides reveal the molecular mechanism underlying the specific and phosphorylation-dependent Dlg/Lgl complex formation. In addition to providing a mechanistic basis underlying the regulated formation of the Scribble complex, the structure of the Dlg/Lgl complex may also serve as a starting point for designing specific Dlg inhibitors for targeting the Scribble complex formation.Cell Research advance online publication 11 February 2014; doi:10.1038/cr.2014.16.

Phosphorylation-dependent interaction between tumor suppressors Dlg and Lgl.,Zhu J, Shang Y, Wan Q, Xia Y, Chen J, Du Q, Zhang M Cell Res. 2014 Feb 11. doi: 10.1038/cr.2014.16. PMID:24513855^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hruska-Hageman AM, Benson CJ, Leonard AS, Price MP, Welsh MJ. PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current. J Biol Chem. 2004 Nov 5;279(45):46962-8. Epub 2004 Aug 17. PMID:15317815 doi:10.1074/jbc.M405874200
↑ Prange O, Wong TP, Gerrow K, Wang YT, El-Husseini A. A balance between excitatory and inhibitory synapses is controlled by PSD-95 and neuroligin. Proc Natl Acad Sci U S A. 2004 Sep 21;101(38):13915-20. Epub 2004 Sep 9. PMID:15358863 doi:10.1073/pnas.0405939101
↑ Zhu J, Shang Y, Wan Q, Xia Y, Chen J, Du Q, Zhang M. Phosphorylation-dependent interaction between tumor suppressors Dlg and Lgl. Cell Res. 2014 Feb 11. doi: 10.1038/cr.2014.16. PMID:24513855 doi:https://dx.doi.org/10.1038/cr.2014.16

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Hruska-Hageman AM, Benson CJ, Leonard AS, Price MP, Welsh MJ. PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current. J Biol Chem. 2004 Nov 5;279(45):46962-8. Epub 2004 Aug 17. PMID:15317815 doi:10.1074/jbc.M405874200

[2] Prange O, Wong TP, Gerrow K, Wang YT, El-Husseini A. A balance between excitatory and inhibitory synapses is controlled by PSD-95 and neuroligin. Proc Natl Acad Sci U S A. 2004 Sep 21;101(38):13915-20. Epub 2004 Sep 9. PMID:15358863 doi:10.1073/pnas.0405939101

[3] Zhu J, Shang Y, Wan Q, Xia Y, Chen J, Du Q, Zhang M. Phosphorylation-dependent interaction between tumor suppressors Dlg and Lgl. Cell Res. 2014 Feb 11. doi: 10.1038/cr.2014.16. PMID:24513855 doi:https://dx.doi.org/10.1038/cr.2014.16

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
 ==Phosphorylation-dependent interaction between tumor suppressors Dlg and Lgl==
-<StructureSection load='3wp1' size='340' side='right' caption='[[3wp1]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+<StructureSection load='3wp1' size='340' side='right'caption='[[3wp1]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3wp1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WP1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WP1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3wp1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WP1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WP1 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.804&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wp0|3wp0]]</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=3wp1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wp1 OCA], [https://pdbe.org/3wp1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wp1 RCSB], [https://www.ebi.ac.uk/pdbsum/3wp1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wp1 ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Dlg4, Dlgh4, Psd95 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=3wp1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wp1 OCA], [http://pdbe.org/3wp1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wp1 RCSB], [http://www.ebi.ac.uk/pdbsum/3wp1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wp1 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DLG4_RAT DLG4_RAT]] Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B.<ref>PMID:15317815</ref> <ref>PMID:15358863</ref>  [[http://www.uniprot.org/uniprot/L2GL2_HUMAN L2GL2_HUMAN]] Part of a complex with GPSM2/LGN, PRKCI/aPKC and PARD6B/Par-6, which may ensure the correct organization and orientation of bipolar spindles for normal cell division. This complex plays roles in the initial phase of the establishment of epithelial cell polarity.<ref>PMID:15632202</ref>
+[https://www.uniprot.org/uniprot/DLG4_RAT DLG4_RAT] Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B.<ref>PMID:15317815</ref> <ref>PMID:15358863</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 19: @@
 </div>
 <div class="pdbe-citations 3wp1" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Postsynaptic density protein 3D structures|Postsynaptic density protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
+[[Category: Homo sapiens]]
-[[Category: Chen, J]]
+[[Category: Large Structures]]
-[[Category: Du, Q]]
+[[Category: Rattus norvegicus]]
-[[Category: Shang, Y]]
+[[Category: Chen J]]
-[[Category: Wan, Q]]
+[[Category: Du Q]]
-[[Category: Xia, Y]]
+[[Category: Shang Y]]
-[[Category: Zhang, M]]
+[[Category: Wan Q]]
-[[Category: Zhu, J]]
+[[Category: Xia Y]]
-[[Category: Cell polarity]]
+[[Category: Zhang M]]
-[[Category: Maguk]]
+[[Category: Zhu J]]
-[[Category: Peptide binding protein]]
-[[Category: Phosphorylation]]
-[[Category: Phosphorylation dependent]]
-[[Category: Tumor suppressor]]

3wp1: Difference between revisions

Latest revision as of 06:18, 17 October 2024

Phosphorylation-dependent interaction between tumor suppressors Dlg and Lgl

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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