8p0w
From Proteopedia
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/COMD1_HUMAN COMD1_HUMAN] Promotes ubiquitination of NF-kappa-B subunit RELA and its subsequent proteasomal degradation. Down-regulates NF-kappa-B activity. Down-regulates SOD1 activity by interfering with its homodimerization. Plays a role in copper ion homeostasis. Can bind one copper ion per monomer. May function to facilitate biliary copper excretion within hepatocytes.<ref>PMID:14685266</ref> <ref>PMID:15799966</ref> <ref>PMID:16573520</ref> <ref>PMID:17309234</ref> <ref>PMID:17183367</ref> <ref>PMID:20048074</ref> <ref>PMID:20595380</ref> | [https://www.uniprot.org/uniprot/COMD1_HUMAN COMD1_HUMAN] Promotes ubiquitination of NF-kappa-B subunit RELA and its subsequent proteasomal degradation. Down-regulates NF-kappa-B activity. Down-regulates SOD1 activity by interfering with its homodimerization. Plays a role in copper ion homeostasis. Can bind one copper ion per monomer. May function to facilitate biliary copper excretion within hepatocytes.<ref>PMID:14685266</ref> <ref>PMID:15799966</ref> <ref>PMID:16573520</ref> <ref>PMID:17309234</ref> <ref>PMID:17183367</ref> <ref>PMID:20048074</ref> <ref>PMID:20595380</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The Commander complex, a 16-protein assembly, plays multiple roles in cell homeostasis, cell cycle and immune response. It consists of copper-metabolism Murr1 domain proteins (COMMD1-10), coiled-coil domain-containing proteins (CCDC22 and CCDC93), DENND10 and the Retriever subcomplex (VPS26C, VPS29 and VPS35L), all expressed ubiquitously in the body and linked to various diseases. Here, we report the structure and key interactions of the endogenous human Commander complex by cryogenic-electron microscopy and mass spectrometry-based proteomics. The complex consists of a stable core of COMMD1-10 and an effector containing DENND10 and Retriever, scaffolded together by CCDC22 and CCDC93. We establish the composition of Commander and reveal major interaction interfaces. These findings clarify its roles in intracellular transport, and uncover a strong association with cilium assembly, and centrosome and centriole functions. | ||
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| + | Structure and interactions of the endogenous human Commander complex.,Laulumaa S, Kumpula EP, Huiskonen JT, Varjosalo M Nat Struct Mol Biol. 2024 Jun;31(6):925-938. doi: 10.1038/s41594-024-01246-1. , Epub 2024 Mar 8. PMID:38459129<ref>PMID:38459129</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8p0w" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Structure of the human Commander complex COMMD ring
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