9y75: Difference between revisions

Latest revision as of 08:48, 16 September 2026

Cryo-EM structure of ML-SA1-bound full-length mouse TRPML2 channel in lipid nanodisc, closed IV

Structural highlights

9y75 is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.47Å
Ligands:	AQV
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MCLN2_MOUSE Nonselective cation channel probably playing a role in the regulation of membrane trafficking events. Acts as a Ca(2+)-permeable cation channel with inwardly rectifying activity (PubMed:19763610). May activate ARF6 and be involved in the trafficking of GPI-anchored cargo proteins to the cell surface via the ARF6-regulated recycling pathway (By similarity). May play a role in immune processes. In adaptive immunity, TRPML2 and TRPML1 may play redundant roles in the function of the specialized lysosomes of B cells (PubMed:17050035). In the innate immune response, may play a role in the regulation of chemokine secretion and macrophage migration (PubMed:26432893). Through a possible and probably tissue-specific heteromerization with MCOLN1 may be at least in part involved in many lysosome-dependent cellular events. Also functions as a Fe(2+) permeable channel (PubMed:18794901).[UniProtKB:Q8IZK6]^[1] ^[2] ^[3] ^[4] ^[5]

References

↑ Song Y, Dayalu R, Matthews SA, Scharenberg AM. TRPML cation channels regulate the specialized lysosomal compartment of vertebrate B-lymphocytes. Eur J Cell Biol. 2006 Dec;85(12):1253-64. Epub 2006 Oct 16. PMID:17050035 doi:https://dx.doi.org/10.1016/j.ejcb.2006.08.004
↑ Dong XP, Cheng X, Mills E, Delling M, Wang F, Kurz T, Xu H. The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel. Nature. 2008 Oct 16;455(7215):992-6. doi: 10.1038/nature07311. Epub 2008 Sep 14. PMID:18794901 doi:https://dx.doi.org/10.1038/nature07311
↑ Samie MA, Grimm C, Evans JA, Curcio-Morelli C, Heller S, Slaugenhaupt SA, Cuajungco MP. The tissue-specific expression of TRPML2 (MCOLN-2) gene is influenced by the presence of TRPML1. Pflugers Arch. 2009 Nov;459(1):79-91. doi: 10.1007/s00424-009-0716-5. PMID:19763610 doi:https://dx.doi.org/10.1007/s00424-009-0716-5
↑ Grimm C, Jors S, Guo Z, Obukhov AG, Heller S. Constitutive activity of TRPML2 and TRPML3 channels versus activation by low extracellular sodium and small molecules. J Biol Chem. 2012 Jun 29;287(27):22701-8. doi: 10.1074/jbc.M112.368876. PMID:22753890 doi:https://dx.doi.org/10.1074/jbc.M112.368876
↑ Sun L, Hua Y, Vergarajauregui S, Diab HI, Puertollano R. Novel Role of TRPML2 in the Regulation of the Innate Immune Response. J Immunol. 2015 Nov 15;195(10):4922-32. doi: 10.4049/jimmunol.1500163. Epub 2015 , Oct 2. PMID:26432893 doi:https://dx.doi.org/10.4049/jimmunol.1500163

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OCA

[1] Song Y, Dayalu R, Matthews SA, Scharenberg AM. TRPML cation channels regulate the specialized lysosomal compartment of vertebrate B-lymphocytes. Eur J Cell Biol. 2006 Dec;85(12):1253-64. Epub 2006 Oct 16. PMID:17050035 doi:https://dx.doi.org/10.1016/j.ejcb.2006.08.004

[2] Dong XP, Cheng X, Mills E, Delling M, Wang F, Kurz T, Xu H. The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel. Nature. 2008 Oct 16;455(7215):992-6. doi: 10.1038/nature07311. Epub 2008 Sep 14. PMID:18794901 doi:https://dx.doi.org/10.1038/nature07311

[3] Samie MA, Grimm C, Evans JA, Curcio-Morelli C, Heller S, Slaugenhaupt SA, Cuajungco MP. The tissue-specific expression of TRPML2 (MCOLN-2) gene is influenced by the presence of TRPML1. Pflugers Arch. 2009 Nov;459(1):79-91. doi: 10.1007/s00424-009-0716-5. PMID:19763610 doi:https://dx.doi.org/10.1007/s00424-009-0716-5

[4] Grimm C, Jors S, Guo Z, Obukhov AG, Heller S. Constitutive activity of TRPML2 and TRPML3 channels versus activation by low extracellular sodium and small molecules. J Biol Chem. 2012 Jun 29;287(27):22701-8. doi: 10.1074/jbc.M112.368876. PMID:22753890 doi:https://dx.doi.org/10.1074/jbc.M112.368876

[5] Sun L, Hua Y, Vergarajauregui S, Diab HI, Puertollano R. Novel Role of TRPML2 in the Regulation of the Innate Immune Response. J Immunol. 2015 Nov 15;195(10):4922-32. doi: 10.4049/jimmunol.1500163. Epub 2015 , Oct 2. PMID:26432893 doi:https://dx.doi.org/10.4049/jimmunol.1500163

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 9y75 is ON HOLD  until Paper Publication
+==Cryo-EM structure of ML-SA1-bound full-length mouse TRPML2 channel in lipid nanodisc, closed IV==
+<StructureSection load='9y75' size='340' side='right'caption='[[9y75]], [[Resolution|resolution]] 3.47&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[9y75]] 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=9Y75 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9Y75 FirstGlance]. <br>
-Description:
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.47&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AQV:2-[2-oxidanylidene-2-[(4~{S})-2,2,4-trimethyl-3,4-dihydroquinolin-1-yl]ethyl]isoindole-1,3-dione'>AQV</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=9y75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9y75 OCA], [https://pdbe.org/9y75 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9y75 RCSB], [https://www.ebi.ac.uk/pdbsum/9y75 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9y75 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MCLN2_MOUSE MCLN2_MOUSE] Nonselective cation channel probably playing a role in the regulation of membrane trafficking events. Acts as a Ca(2+)-permeable cation channel with inwardly rectifying activity (PubMed:19763610). May activate ARF6 and be involved in the trafficking of GPI-anchored cargo proteins to the cell surface via the ARF6-regulated recycling pathway (By similarity). May play a role in immune processes. In adaptive immunity, TRPML2 and TRPML1 may play redundant roles in the function of the specialized lysosomes of B cells (PubMed:17050035). In the innate immune response, may play a role in the regulation of chemokine secretion and macrophage migration (PubMed:26432893). Through a possible and probably tissue-specific heteromerization with MCOLN1 may be at least in part involved in many lysosome-dependent cellular events. Also functions as a Fe(2+) permeable channel (PubMed:18794901).[UniProtKB:Q8IZK6]<ref>PMID:17050035</ref> <ref>PMID:18794901</ref> <ref>PMID:19763610</ref> <ref>PMID:22753890</ref> <ref>PMID:26432893</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Mus musculus]]
+[[Category: Park S]]
+[[Category: Yang J]]

9y75: Difference between revisions

Latest revision as of 08:48, 16 September 2026

Cryo-EM structure of ML-SA1-bound full-length mouse TRPML2 channel in lipid nanodisc, closed IV

Structural highlights

Function

References

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