View source for 9mpu


==Cryo-EM structure of p47 bound to VCP N-domain (with D1 domain)==
<StructureSection load='9mpu' size='340' side='right'caption='[[9mpu]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9mpu]] is a 2 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=9MPU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9MPU 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]] 4&#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=9mpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9mpu OCA], [https://pdbe.org/9mpu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9mpu RCSB], [https://www.ebi.ac.uk/pdbsum/9mpu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9mpu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NSF1C_HUMAN NSF1C_HUMAN] Reduces the ATPase activity of VCP. Necessary for the fragmentation of Golgi stacks during mitosis and for VCP-mediated reassembly of Golgi stacks after mitosis. May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER) (By similarity). Inhibits the activity of CTSL (in vitro).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
VCP/p97 regulates a wide range of cellular processes, including post-mitotic Golgi reassembly. In this context, VCP is assisted by p47, an adapter protein, and VCPIP1, a deubiquitylase (DUB). However, how they organize into a functional ternary complex to promote Golgi assembly remains unknown. Here, we use cryo-EM to characterize both VCP-VCPIP1 and VCP-VCPIP1-p47 complexes. We show that VCPIP1 engages VCP through two interfaces: one involving the N-domain of VCP and the UBX domain of VCPIP1, and the other involving the VCP D2 domains and a region of VCPIP1 we refer to as VCPID. The p47 UBX domain competitively binds to the VCP N-domain, while not affecting VCPID binding. We show that VCPID is critical for VCP-mediated enhancement of DUB activity and proper Golgi assembly. The ternary structure along with biochemical and cellular data provides new insights into the complex interplay of VCP with its co-factors.

Structural basis of VCP-VCPIP1-p47 ternary complex in Golgi maintenance.,Shah B, Hunkeler M, Bratt A, Yue H, Jaen Maisonet I, Fischer ES, Buhrlage SJ Nat Commun. 2025 Aug 28;16(1):8025. doi: 10.1038/s41467-025-63161-3. PMID:40877265<ref>PMID:40877265</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9mpu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Buhrlage SJ]]
[[Category: Fischer EF]]
[[Category: Hunkeler M]]
[[Category: Shah B]]