View source for 9qpq


==The structure of the COPI leaf bound to GOLPH3==
<StructureSection load='9qpq' size='340' side='right'caption='[[9qpq]], [[Resolution|resolution]] 7.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9qpq]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9QPQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9QPQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7.5&#8491;</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=9qpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9qpq OCA], [https://pdbe.org/9qpq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9qpq RCSB], [https://www.ebi.ac.uk/pdbsum/9qpq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9qpq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GOLP3_HUMAN GOLP3_HUMAN] Mediates the cis and medial Golgi localization of mannosyltransferases through direct binding of their cytosolic domains. Involved in modulation of mTOR signaling. Involved in the regulation of mitochondrial lipids, leading to increase of mitochondrial mass. Potential oncogene.<ref>PMID:16263763</ref> <ref>PMID:19553991</ref> <ref>PMID:20026658</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The multiple cisternae of the Golgi apparatus contain resident membrane proteins crucial for lipid and protein glycosylation. How Golgi residents remain in their designated compartments despite a constant flow of secretory cargo is incompletely understood. Here, we determine the structure of the COPI vesicle coat containing GOLPH3, an adaptor protein that binds the cytosolic tails of many Golgi residents. Analysis of this structure, together with structure-guided mutagenesis and functional assays, reveals how GOLPH3 uses coincidence detection of COPI and lipids to engage Golgi residents preferentially at late cisternae. Our findings rationalize the logic of cisternal maturation and explain how COPI can engage different types of substrates in different Golgi cisternae to retrieve some proteins back to the ER while retaining others within the Golgi apparatus.

The mechanistic basis of cargo selection during Golgi maturation.,Taylor RJ, Zubkov N, Ciazynska KA, Kaufman JGG, Tagiltsev G, Owen DJ, Briggs JAG, Munro S Sci Adv. 2025 Oct 3;11(40):eaea0016. doi: 10.1126/sciadv.aea0016. Epub 2025 Oct , 3. PMID:41042862<ref>PMID:41042862</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9qpq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Briggs JAG]]
[[Category: Ciazynska KA]]
[[Category: Tagiltsev G]]
[[Category: Taylor RJ]]