5aaq: Difference between revisions
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==TBK1 recruitment to cytosol-invading Salmonella induces anti- bacterial autophagy== | |||
<StructureSection load='5aaq' size='340' side='right' caption='[[5aaq]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5aaq]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AAQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AAQ FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5aas|5aas]], [[5aay|5aay]], [[5aaz|5aaz]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5aaq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aaq OCA], [http://pdbe.org/5aaq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aaq RCSB], [http://www.ebi.ac.uk/pdbsum/5aaq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5aaq ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/CACO2_HUMAN CACO2_HUMAN]] May play a role in ruffle formation and actin cytoskeleton organization. Seems to negatively regulate constitutive secretion.<ref>PMID:17635994</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Mammalian cells deploy autophagy to defend their cytosol against bacterial invaders. Anti-bacterial autophagy relies on the core autophagy machinery, cargo receptors, and "eat-me" signals such as galectin-8 and ubiquitin that label bacteria as autophagy cargo. Anti-bacterial autophagy also requires the kinase TBK1, whose role in autophagy has remained enigmatic. Here we show that recruitment of WIPI2, itself essential for anti-bacterial autophagy, is dependent on the localization of catalytically active TBK1 to the vicinity of cytosolic bacteria. Experimental manipulation of TBK1 recruitment revealed that engagement of TBK1 with any of a variety of Salmonella-associated "eat-me" signals, including host-derived glycans and K48- and K63-linked ubiquitin chains, suffices to restrict bacterial proliferation. Promiscuity in recruiting TBK1 via independent signals may buffer TBK1 functionality from potential bacterial antagonism and thus be of evolutionary advantage to the host. | |||
Recruitment of TBK1 to cytosol-invading Salmonella induces WIPI2-dependent antibacterial autophagy.,Thurston TL, Boyle KB, Allen M, Ravenhill BJ, Karpiyevich M, Bloor S, Kaul A, Noad J, Foeglein A, Matthews SA, Komander D, Bycroft M, Randow F EMBO J. 2016 Jul 1. pii: e201694491. PMID:27370208<ref>PMID:27370208</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5aaq" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Allen, M D]] | |||
[[Category: Bloor, S]] | |||
[[Category: Bycroft, M]] | |||
[[Category: Holden, D]] | [[Category: Holden, D]] | ||
[[Category: | [[Category: Karpiyevitch, M]] | ||
[[Category: Kaul, A]] | [[Category: Kaul, A]] | ||
[[Category: Komander, D]] | [[Category: Komander, D]] | ||
[[Category: Matthews, S]] | |||
[[Category: Randow, F]] | |||
[[Category: Ravenhill, B]] | [[Category: Ravenhill, B]] | ||
[[Category: Thurston, T | [[Category: Thurston, T L]] | ||
[[Category: | [[Category: Calcium-binding protein]] | ||
[[Category: Ndp52]] | |||
[[Category: Tbk1]] | |||
[[Category: Zinc-finger]] | |||
Revision as of 14:40, 14 July 2016
TBK1 recruitment to cytosol-invading Salmonella induces anti- bacterial autophagyTBK1 recruitment to cytosol-invading Salmonella induces anti- bacterial autophagy
Structural highlights
Function[CACO2_HUMAN] May play a role in ruffle formation and actin cytoskeleton organization. Seems to negatively regulate constitutive secretion.[1] Publication Abstract from PubMedMammalian cells deploy autophagy to defend their cytosol against bacterial invaders. Anti-bacterial autophagy relies on the core autophagy machinery, cargo receptors, and "eat-me" signals such as galectin-8 and ubiquitin that label bacteria as autophagy cargo. Anti-bacterial autophagy also requires the kinase TBK1, whose role in autophagy has remained enigmatic. Here we show that recruitment of WIPI2, itself essential for anti-bacterial autophagy, is dependent on the localization of catalytically active TBK1 to the vicinity of cytosolic bacteria. Experimental manipulation of TBK1 recruitment revealed that engagement of TBK1 with any of a variety of Salmonella-associated "eat-me" signals, including host-derived glycans and K48- and K63-linked ubiquitin chains, suffices to restrict bacterial proliferation. Promiscuity in recruiting TBK1 via independent signals may buffer TBK1 functionality from potential bacterial antagonism and thus be of evolutionary advantage to the host. Recruitment of TBK1 to cytosol-invading Salmonella induces WIPI2-dependent antibacterial autophagy.,Thurston TL, Boyle KB, Allen M, Ravenhill BJ, Karpiyevich M, Bloor S, Kaul A, Noad J, Foeglein A, Matthews SA, Komander D, Bycroft M, Randow F EMBO J. 2016 Jul 1. pii: e201694491. PMID:27370208[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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