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6tqt

From Proteopedia

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Current revision

The crystal structure of the MSP domain of human MOSPD2.

Structural highlights

6tqt is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.5Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MSPD2_HUMAN Endoplasmic reticulum-anchored receptor which modulates interorganelle contacts by interacting with other organelle-bound proteins via their FFAT motif (PubMed:29858488). Might have a more important role in endoplasmic reticulum and endosomes contacts (PubMed:29858488). Promotes migration of primary monocytes and neutrophils, in response to various chemokines (PubMed:28137892).^[1] ^[2]

Publication Abstract from PubMed

Organelles are physically connected in membrane contact sites. The endoplasmic reticulum possesses three major receptors, VAP-A, VAP-B, and MOSPD2, which interact with proteins at the surface of other organelles to build contacts. VAP-A, VAP-B, and MOSPD2 contain an MSP domain, which binds a motif named FFAT (two phenylalanines in an acidic tract). In this study, we identified a non-conventional FFAT motif where a conserved acidic residue is replaced by a serine/threonine. We show that phosphorylation of this serine/threonine is critical for non-conventional FFAT motifs (named Phospho-FFAT) to be recognized by the MSP domain. Moreover, structural analyses of the MSP domain alone or in complex with conventional and Phospho-FFAT peptides revealed new mechanisms of interaction. Based on these new insights, we produced a novel prediction algorithm, which expands the repertoire of candidate proteins with a Phospho-FFAT that are able to create membrane contact sites. Using a prototypical tethering complex made by STARD3 and VAP, we showed that phosphorylation is instrumental for the formation of ER-endosome contacts, and their sterol transfer function. This study reveals that phosphorylation acts as a general switch for inter-organelle contacts.

FFAT motif phosphorylation controls formation and lipid transfer function of inter-organelle contacts.,Di Mattia T, Martinet A, Ikhlef S, McEwen AG, Nomine Y, Wendling C, Poussin-Courmontagne P, Voilquin L, Eberling P, Ruffenach F, Cavarelli J, Slee J, Levine TP, Drin G, Tomasetto C, Alpy F EMBO J. 2020 Oct 30:e104369. doi: 10.15252/embj.2019104369. PMID:33124732^[3]

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

References

↑ Mendel I, Yacov N, Salem Y, Propheta-Meiran O, Ishai E, Breitbart E. Identification of Motile Sperm Domain-Containing Protein 2 as Regulator of Human Monocyte Migration. J Immunol. 2017 Mar 1;198(5):2125-2132. doi: 10.4049/jimmunol.1601662. Epub 2017 , Jan 30. PMID:28137892 doi:http://dx.doi.org/10.4049/jimmunol.1601662
↑ Di Mattia T, Wilhelm LP, Ikhlef S, Wendling C, Spehner D, Nomine Y, Giordano F, Mathelin C, Drin G, Tomasetto C, Alpy F. Identification of MOSPD2, a novel scaffold for endoplasmic reticulum membrane contact sites. EMBO Rep. 2018 Jul;19(7). pii: embr.201745453. doi: 10.15252/embr.201745453. Epub, 2018 Jun 1. PMID:29858488 doi:http://dx.doi.org/10.15252/embr.201745453
↑ Di Mattia T, Martinet A, Ikhlef S, McEwen AG, Nomine Y, Wendling C, Poussin-Courmontagne P, Voilquin L, Eberling P, Ruffenach F, Cavarelli J, Slee J, Levine TP, Drin G, Tomasetto C, Alpy F. FFAT motif phosphorylation controls formation and lipid transfer function of inter-organelle contacts. EMBO J. 2020 Oct 30:e104369. doi: 10.15252/embj.2019104369. PMID:33124732 doi:http://dx.doi.org/10.15252/embj.2019104369

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6tqt"

@@ Line 3: / Line 3: @@
 <StructureSection load='6tqt' size='340' side='right'caption='[[6tqt]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6tqt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TQT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TQT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6tqt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TQT FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.5&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MOSPD2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6tqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tqt OCA], [http://pdbe.org/6tqt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tqt RCSB], [http://www.ebi.ac.uk/pdbsum/6tqt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tqt ProSAT]</span></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=6tqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tqt OCA], [https://pdbe.org/6tqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tqt RCSB], [https://www.ebi.ac.uk/pdbsum/6tqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tqt ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MSPD2_HUMAN MSPD2_HUMAN]] Endoplasmic reticulum-anchored receptor which modulates interorganelle contacts by interacting with other organelle-bound proteins via their FFAT motif (PubMed:29858488). Might have a more important role in endoplasmic reticulum and endosomes contacts (PubMed:29858488). Promotes migration of primary monocytes and neutrophils, in response to various chemokines (PubMed:28137892).<ref>PMID:28137892</ref> <ref>PMID:29858488</ref>
+[https://www.uniprot.org/uniprot/MSPD2_HUMAN MSPD2_HUMAN] Endoplasmic reticulum-anchored receptor which modulates interorganelle contacts by interacting with other organelle-bound proteins via their FFAT motif (PubMed:29858488). Might have a more important role in endoplasmic reticulum and endosomes contacts (PubMed:29858488). Promotes migration of primary monocytes and neutrophils, in response to various chemokines (PubMed:28137892).<ref>PMID:28137892</ref> <ref>PMID:29858488</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Alpy, F]]
+[[Category: Alpy F]]
-[[Category: Cavarelli, J]]
+[[Category: Cavarelli J]]
-[[Category: Mattia, T Di]]
+[[Category: Di Mattia T]]
-[[Category: McEwen, A G]]
+[[Category: McEwen AG]]
-[[Category: Poussin-Courmontagne, P]]
+[[Category: Poussin-Courmontagne P]]
-[[Category: Tomasetto, C]]
+[[Category: Tomasetto C]]
-[[Category: Wendling, C]]
+[[Category: Wendling C]]
-[[Category: Endoplasmic reticulum]]
-[[Category: Ffat motif]]
-[[Category: Membrane contact site]]
-[[Category: Msp domain]]
-[[Category: Protein binding]]

6tqt

From Proteopedia

Current revision

The crystal structure of the MSP domain of human MOSPD2.

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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