5ep6
From Proteopedia
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/AZI2_HUMAN AZI2_HUMAN] Adapter protein which binds TBK1 and IKBKE playing a role in antiviral innate immunity. Activates serine/threonine-protein kinase TBK1 and facilitates its oligomerization. Enhances the phosphorylation of NF-kappa-B p65 subunit RELA by TBK1. Promotes TBK1-induced as well as TNF-alpha or PMA-induced activation of NF-kappa-B. Participates in IFNB promoter activation via TICAM1.<ref>PMID:14560022</ref> <ref>PMID:15611223</ref> <ref>PMID:21931631</ref> | [https://www.uniprot.org/uniprot/AZI2_HUMAN AZI2_HUMAN] Adapter protein which binds TBK1 and IKBKE playing a role in antiviral innate immunity. Activates serine/threonine-protein kinase TBK1 and facilitates its oligomerization. Enhances the phosphorylation of NF-kappa-B p65 subunit RELA by TBK1. Promotes TBK1-induced as well as TNF-alpha or PMA-induced activation of NF-kappa-B. Participates in IFNB promoter activation via TICAM1.<ref>PMID:14560022</ref> <ref>PMID:15611223</ref> <ref>PMID:21931631</ref> | ||
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| - | == Publication Abstract from PubMed == | ||
| - | Optineurin is an important autophagy receptor involved in several selective autophagy processes, during which its function is regulated by TBK1. Mutations of optineurin and TBK1 are both associated with neurodegenerative diseases. However, the mechanistic basis underlying the specific interaction between optineurin and TBK1 is still elusive. Here we determine the crystal structures of optineurin/TBK1 complex and the related NAP1/TBK1 complex, uncovering the detailed molecular mechanism governing the optineurin and TBK1 interaction, and revealing a general binding mode between TBK1 and its associated adaptor proteins. In addition, we demonstrate that the glaucoma-associated optineurin E50K mutation not only enhances the interaction between optineurin and TBK1 but also alters the oligomeric state of optineurin, and the ALS-related TBK1 E696K mutation specifically disrupts the optineurin/TBK1 complex formation but has little effect on the NAP1/TBK1 complex. Thus, our study provides mechanistic insights into those currently known disease-causing optineurin and TBK1 mutations found in patients. | ||
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| - | Structural insights into the interaction and disease mechanism of neurodegenerative disease-associated optineurin and TBK1 proteins.,Li F, Xie X, Wang Y, Liu J, Cheng X, Guo Y, Gong Y, Hu S, Pan L Nat Commun. 2016 Sep 13;7:12708. doi: 10.1038/ncomms12708. PMID:27620379<ref>PMID:27620379</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
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| - | <div class="pdbe-citations 5ep6" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
The crystal structure of NAP1 in complex with TBK1
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Categories: Homo sapiens | Large Structures | Li F | Liu J | Pan L | Xie X
