{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T21:50:27Z","timestamp":1777413027663,"version":"3.51.4"},"reference-count":165,"publisher":"Elsevier BV","issue":"6","license":[{"start":{"date-parts":[[2021,12,1]],"date-time":"2021-12-01T00:00:00Z","timestamp":1638316800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,12,1]],"date-time":"2021-12-01T00:00:00Z","timestamp":1638316800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2021,10,20]],"date-time":"2021-10-20T00:00:00Z","timestamp":1634688000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"NIH","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2021,12]]},"DOI":"10.1016\/j.jbc.2021.101340","type":"journal-article","created":{"date-parts":[[2021,10,25]],"date-time":"2021-10-25T07:14:55Z","timestamp":1635146095000},"page":"101340","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":21,"title":["The unity of opposites: Strategic interplay between bacterial effectors to regulate cellular homeostasis"],"prefix":"10.1016","volume":"297","author":[{"given":"Shalini","family":"Iyer","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0567-7753","authenticated-orcid":false,"given":"Chittaranjan","family":"Das","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2021.101340_bib1","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1146\/annurev.cellbio.17.1.53","article-title":"Salmonella interactions with host cells: Type III secretion at work","volume":"17","author":"Gal\u00e1n","year":"2001","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"10.1016\/j.jbc.2021.101340_bib2","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1146\/annurev.micro.58.030603.123630","article-title":"Biogenesis, architecture, and function of bacterial type iv secretion systems","volume":"59","author":"Christie","year":"2005","journal-title":"Annu. Rev. Microbiol."},{"key":"10.1016\/j.jbc.2021.101340_bib3","doi-asserted-by":"crossref","first-page":"1570","DOI":"10.1099\/mic.0.2008\/016840-0","article-title":"The bacterial type VI secretion machine: Yet another player for protein transport across membranes","volume":"154","author":"Filloux","year":"2008","journal-title":"Microbiology"},{"key":"10.1016\/j.jbc.2021.101340_bib4","first-page":"1","article-title":"Bacterial protein toxins. An overview","volume":"145","author":"Alouf","year":"2000","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.jbc.2021.101340_bib5","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/j.mib.2006.02.008","article-title":"Type IV secretion systems and their effectors in bacterial pathogenesis","volume":"9","author":"Backert","year":"2006","journal-title":"Curr. Opin. Microbiol."},{"key":"10.1016\/j.jbc.2021.101340_bib6","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.mib.2008.11.010","article-title":"The type VI secretion system: Translocation of effectors and effector-domains","volume":"12","author":"Pukatzki","year":"2009","journal-title":"Curr. Opin. Microbiol."},{"key":"10.1016\/j.jbc.2021.101340_bib7","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1111\/j.1365-2958.1993.tb01092.x","article-title":"Two distinct defects in intracellular growth complemented by a single genetic locus in Legionella pneumophila","volume":"7","author":"Berger","year":"1993","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2021.101340_bib8","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1073\/pnas.0304916101","article-title":"Multiple substrates of the Legionella pneumophila Dot\/Icm system identified by interbacterial protein transfer","volume":"101","author":"Luo","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2021.101340_bib9","doi-asserted-by":"crossref","first-page":"9607","DOI":"10.1073\/pnas.89.20.9607","article-title":"Identification of a Legionella pneumophila locus required for intracellular multiplication in human macrophages","volume":"89","author":"Marra","year":"1992","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2021.101340_bib10","doi-asserted-by":"crossref","first-page":"797","DOI":"10.1111\/j.1365-2958.1994.tb01316.x","article-title":"The Legionella pneumophila icm locus: A set of genes required for intracellular multiplication in human macrophages","volume":"14","author":"Brand","year":"1994","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2021.101340_bib11","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1038\/nrmicro.2017.67","article-title":"Legionella and Coxiella effectors: Strength in diversity and activity","volume":"15","author":"Qiu","year":"2017","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.jbc.2021.101340_bib12","doi-asserted-by":"crossref","first-page":"e01201","DOI":"10.1128\/mBio.01201-20","article-title":"Molecular mimicry: A paradigm of host-microbe coevolution illustrated by legionella","volume":"11","author":"Mondino","year":"2020","journal-title":"MBio"},{"key":"10.1016\/j.jbc.2021.101340_bib13","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1038\/45829","article-title":"A\u00a0Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion","volume":"401","author":"Fu","year":"1999","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2021.101340_bib14","doi-asserted-by":"crossref","first-page":"1985","DOI":"10.1242\/jcs.188482","article-title":"Exploitation of the host cell ubiquitin machinery by microbial effector proteins","volume":"130","author":"Lin","year":"2017","journal-title":"J.\u00a0Cell Sci."},{"key":"10.1016\/j.jbc.2021.101340_bib15","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/j.chom.2013.07.008","article-title":"What pathogens have taught us about posttranslational modifications","volume":"14","author":"Salomon","year":"2013","journal-title":"Cell Host Microbe"},{"key":"10.1016\/j.jbc.2021.101340_bib16","doi-asserted-by":"crossref","first-page":"3868","DOI":"10.1002\/1873-3468.12326","article-title":"The life stage-specific pathometabolism of Legionella pneumophila","volume":"590","author":"Eisenreich","year":"2016","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jbc.2021.101340_bib17","doi-asserted-by":"crossref","DOI":"10.3389\/fcell.2018.00001","article-title":"Subversion of the endocytic and secretory pathways by bacterial effector proteins","author":"Weber","year":"2018","journal-title":"Front. Cell Dev. Biol."},{"key":"10.1016\/j.jbc.2021.101340_bib18","doi-asserted-by":"crossref","first-page":"4321","DOI":"10.1016\/j.jmb.2019.07.028","article-title":"Viewing Legionella pneumophila pathogenesis through an immunological lens","volume":"431","author":"Liu","year":"2019","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2021.101340_bib19","doi-asserted-by":"crossref","first-page":"112","DOI":"10.3389\/fmolb.2020.00112","article-title":"Structure, dynamics and cellular insight into novel substrates of the Legionella pneumophila type II secretion system","volume":"7","author":"Portlock","year":"2020","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.jbc.2021.101340_bib20","doi-asserted-by":"crossref","DOI":"10.3389\/fcimb.2020.593823","article-title":"Mechanisms of effector-mediated immunity revealed by the accidental human pathogen Legionella pneumophila","author":"Ngwaga","year":"2021","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"10.1016\/j.jbc.2021.101340_bib21","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1146\/annurev-biochem-060310-170328","article-title":"The ubiquitin code","volume":"81","author":"Komander","year":"2012","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.jbc.2021.101340_bib22","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a003350","article-title":"Signaling to NF- B: Regulation by ubiquitination","volume":"2","author":"Wertz","year":"2010","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.jbc.2021.101340_bib23","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1080\/10409238.2017.1325829","article-title":"Ubiquitin enzymes in the regulation of immune responses","volume":"52","author":"Ebner","year":"2017","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"10.1016\/j.jbc.2021.101340_bib24","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1186\/s12929-019-0569-y","article-title":"Ubiquitin-mediated regulation of autophagy","volume":"26","author":"Chen","year":"2019","journal-title":"J.\u00a0Biomed. Sci."},{"key":"10.1016\/j.jbc.2021.101340_bib25","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1093\/hmg\/ddm320","article-title":"Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases","volume":"17","author":"Tan","year":"2008","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.jbc.2021.101340_bib26","first-page":"227","article-title":"Modulation of the ubiquitination machinery by Legionella","volume":"376","author":"Hubber","year":"2013","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"10.1016\/j.jbc.2021.101340_bib27","doi-asserted-by":"crossref","first-page":"487","DOI":"10.3389\/fcimb.2017.00487","article-title":"Hijacking of the host ubiquitin network by Legionella pneumophila","volume":"7","author":"Qiu","year":"2017","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"10.1016\/j.jbc.2021.101340_bib28","doi-asserted-by":"crossref","first-page":"1636","DOI":"10.1016\/j.cell.2016.11.019","article-title":"Phosphoribosylation of ubiquitin promotes serine ubiquitination and impairs conventional ubiquitination","volume":"167","author":"Bhogaraju","year":"2016","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2021.101340_bib29","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1038\/nature17657","article-title":"Ubiquitination independent of E1 and E2 enzymes by bacterial effectors","volume":"533","author":"Qiu","year":"2016","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2021.101340_bib30","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1038\/s41564-018-0282-8","article-title":"Legionella pneumophila inhibits immune signalling via MavC-mediated transglutaminase-induced ubiquitination of UBE2N","volume":"4","author":"Gan","year":"2019","journal-title":"Nat. Microbiol."},{"key":"10.1016\/j.jbc.2021.101340_bib31","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1038\/nrmicro3259","article-title":"Exploitation of the host ubiquitin system by human bacterial pathogens","volume":"12","author":"Ashida","year":"2014","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.jbc.2021.101340_bib32","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1038\/cr.2016.38","article-title":"Substrate specificity of the ubiquitin and Ubl proteases","volume":"26","author":"Ronau","year":"2016","journal-title":"Cell Res."},{"key":"10.1016\/j.jbc.2021.101340_bib33","doi-asserted-by":"crossref","DOI":"10.15252\/embj.2020105127","article-title":"Identification and characterization of diverse OTU deubiquitinases in bacteria","volume":"39","author":"Schubert","year":"2020","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2021.101340_bib34","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1004255","article-title":"Hell\u2019s BELs: Bacterial E3 ligases that exploit the eukaryotic ubiquitin machinery","volume":"10","author":"Huibregtse","year":"2014","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2021.101340_bib35","doi-asserted-by":"crossref","first-page":"1857","DOI":"10.1042\/BST20190526","article-title":"Bacterial dubs: Deubiquitination beyond the seven classes","volume":"47","author":"Hermanns","year":"2019","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.jbc.2021.101340_bib36","doi-asserted-by":"crossref","first-page":"15090","DOI":"10.1073\/pnas.1514568112","article-title":"Structural basis of substrate recognition by a bacterial deubiquitinase important for dynamics of phagosome ubiquitination","volume":"112","author":"Sheedlo","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2021.101340_bib37","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1126\/science.1193844","article-title":"Glutamine deamidation and dysfunction of ubiquitin\/NEDD8 induced by a bacterial effector family","volume":"329","author":"Cui","year":"2010","journal-title":"Science"},{"key":"10.1016\/j.jbc.2021.101340_bib38","doi-asserted-by":"crossref","first-page":"20395","DOI":"10.1073\/pnas.1210831109","article-title":"Structural mechanism of ubiquitin and NEDD8 deamidation catalyzed by bacterial effectors that induce macrophage-specific apoptosis","volume":"109","author":"Yao","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2021.101340_bib39","doi-asserted-by":"crossref","first-page":"568","DOI":"10.1016\/j.celrep.2018.03.060","article-title":"Discovery of ubiquitin deamidases in the pathogenic arsenal of Legionella pneumophila","volume":"23","author":"Valleau","year":"2018","journal-title":"Cell Rep."},{"key":"10.1016\/j.jbc.2021.101340_bib40","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1016\/S0092-8674(00)00126-4","article-title":"Activation of the I\u03bab kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain","volume":"103","author":"Deng","year":"2000","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2021.101340_bib41","doi-asserted-by":"crossref","first-page":"2365","DOI":"10.1038\/s41467-020-16211-x","article-title":"Legionella effector MavC targets the Ube2N\u223cUb conjugate for noncanonical ubiquitination","volume":"11","author":"Puvar","year":"2020","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2021.101340_bib42","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1002\/pro.2162","article-title":"Regulation of the activities of the mammalian transglutaminase family of enzymes","volume":"21","author":"Kl\u00f6ock","year":"2012","journal-title":"Protein Sci."},{"key":"10.1016\/j.jbc.2021.101340_bib43","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1021\/acs.biochem.1c00069","article-title":"Acquisition of a mysterious new domain modulates the function of a bacterial effector","volume":"60","author":"Puvar","year":"2021","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2021.101340_bib44","doi-asserted-by":"crossref","DOI":"10.15252\/embj.2019102806","article-title":"Legionella pneumophila regulates the activity of UBE 2N by deamidase-mediated deubiquitination","volume":"39","author":"Gan","year":"2020","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2021.101340_bib45","doi-asserted-by":"crossref","first-page":"1774","DOI":"10.1038\/s41467-020-15645-7","article-title":"Structural insights into the mechanism and inhibition of transglutaminase-induced ubiquitination by the Legionella effector MavC","volume":"11","author":"Mu","year":"2020","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2021.101340_bib46","doi-asserted-by":"crossref","first-page":"2751","DOI":"10.1038\/s41467-020-16587-w","article-title":"Insights into catalysis and regulation of non-canonical ubiquitination and deubiquitination by bacterial deamidase effectors","volume":"11","author":"Wang","year":"2020","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2021.101340_bib47","doi-asserted-by":"crossref","DOI":"10.1002\/advs.202000871","article-title":"Molecular basis of ubiquitination catalyzed by the bacterial transglutaminase MavC","author":"Guan","year":"2020","journal-title":"Adv. Sci."},{"key":"10.1016\/j.jbc.2021.101340_bib48","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1038\/nsmb1148","article-title":"Mms2-Ubc13 covalently bound to ubiquitin reveals the structural basis of linkage-specific polyubiquitin chain formation","volume":"13","author":"Eddins","year":"2006","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.jbc.2021.101340_bib49","doi-asserted-by":"crossref","first-page":"9448","DOI":"10.1074\/jbc.M211240200","article-title":"Protein interactions within the N-end rule ubiquitin ligation pathway","volume":"278","author":"Siepmann","year":"2003","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101340_bib50","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1038\/cr.2016.35","article-title":"E2 enzymes: More than just middle men","volume":"26","author":"Stewart","year":"2016","journal-title":"Cell Res."},{"key":"10.1016\/j.jbc.2021.101340_bib51","doi-asserted-by":"crossref","first-page":"2623","DOI":"10.1016\/j.jmb.2013.02.037","article-title":"Structural basis for the recognition of Ubc13 by the Shigella flexneri effector ospi","volume":"425","author":"Nishide","year":"2013","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2021.101340_bib52","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1003322","article-title":"Complex structure of OspI and Ubc13: The molecular basis of Ubc13 deamidation and convergence of bacterial and host E2 recognition","volume":"9","author":"Fu","year":"2013","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2021.101340_bib53","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1038\/nrm2780","article-title":"Building ubiquitin chains: E2 enzymes at work","volume":"10","author":"Ye","year":"2009","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.jbc.2021.101340_bib54","doi-asserted-by":"crossref","first-page":"1106","DOI":"10.1111\/j.1742-4658.2012.08507.x","article-title":"Contribution of active site glutamine to rate enhancement in ubiquitin C-terminal hydrolases","volume":"279","author":"Boudreaux","year":"2012","journal-title":"FEBS J."},{"key":"10.1016\/j.jbc.2021.101340_bib55","doi-asserted-by":"crossref","first-page":"64471","DOI":"10.18632\/oncotarget.10948","article-title":"Ubc13: The Lys63 ubiquitin chain building machine","volume":"7","author":"Hodge","year":"2016","journal-title":"Oncotarget"},{"key":"10.1016\/j.jbc.2021.101340_bib56","doi-asserted-by":"crossref","first-page":"2177","DOI":"10.1084\/jem.20060766","article-title":"NF-\u03baB translocation prevents host cell death after low-dose challenge by Legionella pneumophila","volume":"203","author":"Losick","year":"2006","journal-title":"J.\u00a0Exp. Med."},{"key":"10.1016\/j.jbc.2021.101340_bib57","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1093\/nar\/28.1.27","article-title":"KEGG: Kyoto encyclopedia of genes and genomes","volume":"28","author":"Kanehisa","year":"2000","journal-title":"Nucl. Acids Res."},{"key":"10.1016\/j.jbc.2021.101340_bib58","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1038\/nrm2728","article-title":"Rab GTPases as coordinators of vesicle traffic","volume":"10","author":"Stenmark","year":"2009","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.jbc.2021.101340_bib59","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1080\/21541248.2016.1276999","article-title":"Molecular control of Rab activity by GEFs, GAPs and GDI","volume":"9","author":"M\u00fcller","year":"2018","journal-title":"Small GTPases"},{"key":"10.1016\/j.jbc.2021.101340_bib60","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1080\/21541248.2017.1336191","article-title":"Rab GTPases and their interacting protein partners: Structural insights into Rab functional diversity","volume":"9","author":"Pylypenko","year":"2018","journal-title":"Small GTPases"},{"key":"10.1016\/j.jbc.2021.101340_bib61","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1016\/S0968-0004(96)10062-1","article-title":"Structural insights into the function of the Rab GDI superfamily","volume":"21","author":"Wu","year":"1996","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.jbc.2021.101340_bib62","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1128\/MMBR.00023-07","article-title":"Manipulation of Rab GTPase function by intracellular bacterial pathogens","volume":"71","author":"Brumell","year":"2007","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"10.1016\/j.jbc.2021.101340_bib63","doi-asserted-by":"crossref","first-page":"718","DOI":"10.1126\/science.276.5313.718","article-title":"Exploitation of mammalian host cell functions by bacterial pathogens","volume":"276","author":"Finlay","year":"1997","journal-title":"Science"},{"key":"10.1016\/j.jbc.2021.101340_bib64","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1016\/j.chom.2013.08.010","article-title":"A\u00a0Rab-centric perspective of bacterial pathogen-occupied vacuoles","volume":"14","author":"Sherwood","year":"2013","journal-title":"Cell Host Microbe"},{"key":"10.1016\/j.jbc.2021.101340_bib65","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.01623","article-title":"Diversity and plasticity in Rab GTPase nucleotide release mechanism has consequences for Rab activation and inactivation","volume":"3","author":"Langemeyer","year":"2014","journal-title":"Elife"},{"key":"10.1016\/j.jbc.2021.101340_bib66","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1172\/JCI109874","article-title":"Legionnaires\u2019 disease bacterium (Legionella pneumophila) multiples intracellularly in human monocytes","volume":"66","author":"Horwitz","year":"1980","journal-title":"J.\u00a0Clin. Invest."},{"key":"10.1016\/j.jbc.2021.101340_bib67","doi-asserted-by":"crossref","first-page":"2108","DOI":"10.1084\/jem.158.6.2108","article-title":"The legionnaires\u2019 disease bacterium (Legionella pneumophila) inhibits phagosome-lysosome fusion in human monocytes","volume":"158","author":"Horwitz","year":"1983","journal-title":"J.\u00a0Exp. Med."},{"key":"10.1016\/j.jbc.2021.101340_bib68","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1083\/jcb.115.1.31","article-title":"Rab1b regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments","volume":"115","author":"Plutner","year":"1991","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.jbc.2021.101340_bib69","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1016\/0092-8674(88)90433-3","article-title":"The yeast GTP-binding YPT1 protein and a mammalian counterpart are associated with the secretion machinery","volume":"52","author":"Segev","year":"1988","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2021.101340_bib70","doi-asserted-by":"crossref","first-page":"1246","DOI":"10.1111\/j.1600-0854.2010.01086.x","article-title":"Autophagosome formation depends on the small GTPase Rab1 and functional ER exit sites","volume":"11","author":"Zoppino","year":"2010","journal-title":"Traffic"},{"key":"10.1016\/j.jbc.2021.101340_bib71","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.devcel.2006.05.013","article-title":"Targeting of host Rab GTPase function by the intravacuolar pathogen Legionella pneumophila","volume":"11","author":"Machner","year":"2006","journal-title":"Dev. Cell."},{"key":"10.1016\/j.jbc.2021.101340_bib72","doi-asserted-by":"crossref","first-page":"72","DOI":"10.4161\/cib.13857","article-title":"The versatile Legionella effector protein DrrA","volume":"4","author":"Goody","year":"2011","journal-title":"Commun. Integr. Biol."},{"key":"10.1016\/j.jbc.2021.101340_bib73","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1038\/nature06336","article-title":"Legionella pneumophila proteins that regulate Rab1 membrane cycling","volume":"450","author":"Ingmundson","year":"2007","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2021.101340_bib74","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1038\/ncb1463","article-title":"The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor","volume":"8","author":"Murata","year":"2006","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.jbc.2021.101340_bib75","doi-asserted-by":"crossref","first-page":"946","DOI":"10.1126\/science.1192276","article-title":"The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b","volume":"329","author":"M\u00fcller","year":"2010","journal-title":"Science"},{"key":"10.1016\/j.jbc.2021.101340_bib76","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1126\/science.1207193","article-title":"De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila","volume":"333","author":"Neunuebel","year":"2011","journal-title":"Science"},{"key":"10.1016\/j.jbc.2021.101340_bib77","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1038\/nature10307","article-title":"Legionella pneumophila SidD is a deAMPylase that modifies Rab1","volume":"475","author":"Tan","year":"2011","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2021.101340_bib78","doi-asserted-by":"crossref","DOI":"10.1371\/annotation\/2b8e6418-2496-4ffb-b230-95d90b748086","article-title":"Structural basis for Rab1 De-AMPylation by the Legionella pneumophila effector SidD","volume":"9","author":"Chen","year":"2013","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2021.101340_bib79","doi-asserted-by":"crossref","first-page":"28","DOI":"10.4161\/sgtp.18704","article-title":"The taming of a Rab GTPase by Legionella pneumophila","volume":"3","author":"Neunuebel","year":"2012","journal-title":"Small GTPases"},{"key":"10.1016\/j.jbc.2021.101340_bib80","doi-asserted-by":"crossref","first-page":"4699","DOI":"10.1073\/pnas.0914231107","article-title":"Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM\/DrrA","volume":"107","author":"Zhu","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2021.101340_bib81","doi-asserted-by":"crossref","first-page":"4846","DOI":"10.1074\/jbc.M807505200","article-title":"Rab1 guanine nucleotide exchange factor SidM is a major phosphatidylinositol 4-phosphate-binding effector protein of Legionella pneumophila","volume":"284","author":"Brombacher","year":"2009","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101340_bib82","doi-asserted-by":"crossref","first-page":"1060","DOI":"10.1016\/j.molcel.2009.11.014","article-title":"RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity","volume":"36","author":"Schoebel","year":"2009","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2021.101340_bib83","doi-asserted-by":"crossref","first-page":"974","DOI":"10.1126\/science.1149121","article-title":"A\u00a0bifunctional bacterial protein links GDI displacement to Rab1 activation","volume":"318","author":"Machner","year":"2007","journal-title":"Science"},{"key":"10.1016\/j.jbc.2021.101340_bib84","doi-asserted-by":"crossref","first-page":"496","DOI":"10.1038\/emboj.2009.347","article-title":"Structural insights into the dual nucleotide exchange and GDI displacement activity of SidM\/DrrA","volume":"29","author":"Suh","year":"2010","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2021.101340_bib85","doi-asserted-by":"crossref","first-page":"1077","DOI":"10.1006\/jmbi.2000.4010","article-title":"The mammalian Rab family of small GTPases: Definition of family and subfamily sequence motifs suggests a mechanism for functional specificity in the Ras superfamily","volume":"301","author":"Pereira-Leal","year":"2000","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2021.101340_bib86","doi-asserted-by":"crossref","first-page":"646","DOI":"10.1126\/science.1087761","article-title":"Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase","volume":"302","author":"Rak","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.jbc.2021.101340_bib87","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1083\/jcb.201103008","article-title":"The Ras protein superfamily: Evolutionary tree and role of conserved amino acids","volume":"196","author":"Rojas","year":"2012","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.jbc.2021.101340_bib88","doi-asserted-by":"crossref","first-page":"15737","DOI":"10.1002\/anie.201706927","article-title":"Proximity-triggered covalent Stabilization of low-affinity protein complexes in\u00a0vitro and in\u00a0vivo","volume":"56","author":"Cigler","year":"2017","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.jbc.2021.101340_bib89","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1016\/S0969-2126(99)80054-9","article-title":"Structural basis of activation and GTP hydrolysis in Rab proteins","volume":"7","author":"Dumas","year":"1999","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2021.101340_bib90","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.01035-13","article-title":"AMPylation is critical for Rab1 localization to vacuoles containing Legionella pneumophila","volume":"5","author":"Hardiman","year":"2014","journal-title":"MBio"},{"key":"10.1016\/j.jbc.2021.101340_bib91","doi-asserted-by":"crossref","first-page":"642","DOI":"10.1073\/pnas.58.2.642","article-title":"Regulation of glutamine synthetase. VII. Adenylyl glutamine synthetase: A new form of the enzyme with altered regulatory and kinetic properties","volume":"58","author":"Shapiro","year":"1967","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2021.101340_bib92","doi-asserted-by":"crossref","first-page":"9338","DOI":"10.1021\/ja501496d","article-title":"Reaction mechanism of adenylyltransferase DrrA from Legionella pneumophila elucidated by time-resolved fourier transform infrared spectroscopy","volume":"136","author":"Gavriljuk","year":"2014","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2021.101340_bib93","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1008734","article-title":"Structural insight into the membrane targeting domain of the Legionella deAMPylase SidD","volume":"16","author":"Tasc\u00f3n","year":"2020","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2021.101340_bib94","doi-asserted-by":"crossref","first-page":"6798","DOI":"10.1002\/j.1460-2075.1996.tb01071.x","article-title":"Crystal structure of the protein serine\/threonine phosphatase 2C at 2.0 \u00c5 resolution","volume":"15","author":"Das","year":"1996","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2021.101340_bib95","doi-asserted-by":"crossref","first-page":"1947","DOI":"10.1016\/j.str.2004.09.008","article-title":"An alternate conformation and a third metal in PstP\/Ppp, the M. tuberculosis PP2C-family Ser\/Thr protein phosphatase","volume":"12","author":"Pullen","year":"2004","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2021.101340_bib96","doi-asserted-by":"crossref","first-page":"1029","DOI":"10.1016\/j.cell.2012.06.050","article-title":"Structurally distinct bacterial TBC-like GAPs link Arf GTPase to Rab1 inactivation to counteract host defenses","volume":"150","author":"Dong","year":"2012","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2021.101340_bib97","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1038\/nature04847","article-title":"TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism","volume":"442","author":"Pan","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2021.101340_bib98","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1038\/cr.2013.54","article-title":"Structural analyses of Legionella LepB reveal a new GAP fold that catalytically mimics eukaryotic RasGAP","volume":"23","author":"Yu","year":"2013","journal-title":"Cell Res."},{"key":"10.1016\/j.jbc.2021.101340_bib99","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1038\/embor.2012.211","article-title":"Mechanism of Rab1b deactivation by the Legionella pneumophila GAP LepB","volume":"14","author":"Mihai Gazdag","year":"2013","journal-title":"EMBO Rep."},{"key":"10.1016\/j.jbc.2021.101340_bib100","doi-asserted-by":"crossref","first-page":"24000","DOI":"10.1074\/jbc.M113.470625","article-title":"The Legionella pneumophila GTPase activating protein LepB Accelerates Rab1 deactivation by a non-canonical hydrolytic mechanism","volume":"288","author":"Mishra","year":"2013","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101340_bib101","article-title":"Orchestrated delivery of Legionella effectors by the Icm\/Dot secretion system","author":"Allombert","year":"2019","journal-title":"bioRxiv"},{"key":"10.1016\/j.jbc.2021.101340_bib102","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1038\/nature10335","article-title":"Modulation of Rab GTPase function by a protein phosphocholine transferase","volume":"477","author":"Mukherjee","year":"2011","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2021.101340_bib103","doi-asserted-by":"crossref","DOI":"10.1107\/S010876731309942X","article-title":"Structure of the Legionella effector AnkX, an enzyme that diverts the small GTPase Rab1","volume":"69","author":"Campanacci","year":"2013","journal-title":"Acta Crystallogr. Sect. A. Found. Crystallogr."},{"key":"10.1016\/j.jbc.2021.101340_bib104","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.aaz8041","article-title":"Legionella effector AnkX displaces the switch II region for Rab1b phosphocholination","volume":"6","author":"Ernst","year":"2020","journal-title":"Sci. Adv."},{"key":"10.1016\/j.jbc.2021.101340_bib105","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1146\/annurev-micro-102215-095245","article-title":"Biological diversity and molecular plasticity of FIC domain proteins","volume":"70","author":"Harms","year":"2016","journal-title":"Annu. Rev. Microbiol."},{"key":"10.1016\/j.jbc.2021.101340_bib106","doi-asserted-by":"crossref","first-page":"113","DOI":"10.3389\/fmicb.2010.00113","article-title":"AMPylation: Something old is new again","volume":"1","author":"Woolery","year":"2010","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.jbc.2021.101340_bib107","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.tibs.2014.01.001","article-title":"The many faces of Fic: Structural and functional aspects of Fic enzymes","volume":"39","author":"Garcia-Pino","year":"2014","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.jbc.2021.101340_bib108","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1038\/nn.3102","article-title":"Visual neurotransmission in Drosophila requires expression of Fic in glial capitate projections","volume":"15","author":"Rahman","year":"2012","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.jbc.2021.101340_bib109","doi-asserted-by":"crossref","first-page":"1463","DOI":"10.1093\/hmg\/7.9.1463","article-title":"Huntingtin interacts with a family of WW domain proteins","volume":"7","author":"Faber","year":"1998","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.jbc.2021.101340_bib110","doi-asserted-by":"crossref","first-page":"21212","DOI":"10.1073\/pnas.1114023109","article-title":"Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination","volume":"108","author":"Tan","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2021.101340_bib111","doi-asserted-by":"crossref","first-page":"1774","DOI":"10.1038\/emboj.2012.16","article-title":"Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins","volume":"31","author":"Goody","year":"2012","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2021.101340_bib112","doi-asserted-by":"crossref","DOI":"10.1128\/IAI.00153-19","article-title":"Study of Legionella effector domains revealed novel and prevalent phosphatidylinositol 3-phosphate binding domains","volume":"87","author":"Nachmias","year":"2019","journal-title":"Infect. Immun."},{"key":"10.1016\/j.jbc.2021.101340_bib113","doi-asserted-by":"crossref","first-page":"1004","DOI":"10.1038\/nsmb.1867","article-title":"Structural basis of Fic-mediated adenylylation","volume":"17","author":"Xiao","year":"2010","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.jbc.2021.101340_bib114","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1038\/nature03798","article-title":"Structural basis of family-wide Rab GTPase recognition by rabenosyn-5","volume":"436","author":"Eathiraj","year":"2005","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2021.101340_bib115","doi-asserted-by":"crossref","first-page":"2336","DOI":"10.1002\/cbic.201900200","article-title":"Exploring the substrate scope of the bacterial phosphocholine transferase AnkX for versatile protein functionalization","volume":"20","author":"Ochtrop","year":"2019","journal-title":"ChemBioChem"},{"key":"10.1016\/j.jbc.2021.101340_bib116","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1126\/science.289.5478.444","article-title":"Rab1 recruitment of p115 into a cis-SNARE complex: Programming budding COPII vesicles for fusion","volume":"289","author":"Allan","year":"2000","journal-title":"Science"},{"key":"10.1016\/j.jbc.2021.101340_bib117","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1034\/j.1600-0854.2001.1o007.x","article-title":"Rab1 interaction with a GM130 effector complex regulates COPII vesicle cis -Golgi tethering","volume":"2","author":"Moyer","year":"2001","journal-title":"Traffic"},{"key":"10.1016\/j.jbc.2021.101340_bib118","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1093\/embo-reports\/kve065","article-title":"The Golgi matrix protein GM130: A specific interacting partner of the small GTPase Rab1b","volume":"2","author":"Weide","year":"2001","journal-title":"EMBO Rep."},{"key":"10.1016\/j.jbc.2021.101340_bib119","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1038\/s41421-018-0055-9","article-title":"Regulation of the small GTPase Rab1 function by a bacterial glucosyltransferase","volume":"4","author":"Wang","year":"2018","journal-title":"Cell Discov."},{"key":"10.1016\/j.jbc.2021.101340_bib120","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1111\/j.1365-2958.2005.04539.x","article-title":"IcmS-dependent translocation of SdeA into macrophages by the Legionella pneumophila type IV secretion system","volume":"56","author":"Bardill","year":"2005","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2021.101340_bib121","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1016\/j.tibs.2018.11.006","article-title":"Uncovering the structural basis of a new twist in protein ubiquitination","volume":"44","author":"Puvar","year":"2019","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.jbc.2021.101340_bib122","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/j.chom.2016.12.007","article-title":"A\u00a0single Legionella effector catalyzes a multistep ubiquitination pathway to rearrange tubular endoplasmic reticulum for replication","volume":"21","author":"Kotewicz","year":"2017","journal-title":"Cell Host Microbe"},{"key":"10.1016\/j.jbc.2021.101340_bib123","doi-asserted-by":"crossref","first-page":"10538","DOI":"10.1073\/pnas.1402605111","article-title":"The Legionella effector SidC defines a unique family of ubiquitin ligases important for bacterial phagosomal remodeling","volume":"111","author":"Hsu","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2021.101340_bib124","doi-asserted-by":"crossref","first-page":"4762","DOI":"10.1021\/acs.biochem.7b00664","article-title":"Ubiquitin chains modified by the bacterial ligase SdeA are protected from deubiquitinase hydrolysis","volume":"56","author":"Puvar","year":"2017","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2021.101340_bib125","doi-asserted-by":"crossref","first-page":"3506","DOI":"10.1128\/IAI.00497-15","article-title":"Toxicity and SidJ-mediated suppression of toxicity require distinct regions in the SidE family of Legionella pneumophila effectors","volume":"83","author":"Havey","year":"2015","journal-title":"Infect. Immun."},{"key":"10.1016\/j.jbc.2021.101340_bib126","doi-asserted-by":"crossref","first-page":"674","DOI":"10.1038\/s41586-018-0146-7","article-title":"Structural basis of ubiquitin modification by the Legionella effector SdeA","volume":"557","author":"Dong","year":"2018","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2021.101340_bib127","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1016\/j.cell.2018.04.023","article-title":"Structural insights into non-canonical ubiquitination catalyzed by SidE","volume":"173","author":"Wang","year":"2018","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2021.101340_bib128","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1038\/s41586-018-0147-6","article-title":"Mechanism of phosphoribosyl-ubiquitination mediated by a single legionella effector","volume":"557","author":"Akturk","year":"2018","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2021.101340_bib129","doi-asserted-by":"crossref","first-page":"2843","DOI":"10.1016\/j.jmb.2018.05.043","article-title":"Structural and biochemical study of the mono-ADP-ribosyltransferase domain of SdeA, a ubiquitylating\/deubiquitylating enzyme from Legionella pneumophila","volume":"430","author":"Kim","year":"2018","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2021.101340_bib130","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1038\/s41586-018-0145-8","article-title":"Insights into catalysis and function of phosphoribosyl-linked serine ubiquitination","volume":"557","author":"Kalayil","year":"2018","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2021.101340_bib131","doi-asserted-by":"crossref","first-page":"1309","DOI":"10.1021\/acs.biochem.0c00067","article-title":"Fluorescent probes for monitoring serine ubiquitination","volume":"59","author":"Puvar","year":"2020","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2021.101340_bib132","doi-asserted-by":"crossref","first-page":"4267","DOI":"10.1073\/pnas.1217227110","article-title":"Arginine ADP-ribosylation mechanism based on structural snapshots of iota-toxin and actin complex","volume":"110","author":"Tsurumura","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2021.101340_bib133","doi-asserted-by":"crossref","first-page":"1525","DOI":"10.1128\/JB.02606-14","article-title":"Structural basis of functional diversification of the HD-GYP domain revealed by the Pseudomonas aeruginosa PA4781 protein, which displays an unselective bimetallic binding site","volume":"197","author":"Rinaldo","year":"2015","journal-title":"J.\u00a0Bacteriol."},{"key":"10.1016\/j.jbc.2021.101340_bib134","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1128\/IAI.01278-06","article-title":"The Legionella pneumophila effector SidJ is required for efficient recruitment of endoplasmic reticulum proteins to the bacterial phagosome","volume":"75","author":"Liu","year":"2007","journal-title":"Infect. Immun."},{"key":"10.1016\/j.jbc.2021.101340_bib135","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1004695","article-title":"Spatiotemporal regulation of a Legionella pneumophila T4SS substrate by the metaeffector SidJ","volume":"11","author":"Jeong","year":"2015","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2021.101340_bib136","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1016\/j.molcel.2019.10.019","article-title":"Regulation of phosphoribosyl-linked serine ubiquitination by deubiquitinases DupA and DupB","volume":"77","author":"Shin","year":"2020","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2021.101340_bib137","doi-asserted-by":"crossref","first-page":"23518","DOI":"10.1073\/pnas.1916287116","article-title":"Deubiquitination of phosphoribosyl-ubiquitin conjugates by phosphodiesterase-domain\u2013containing Legionella effectors","volume":"116","author":"Wan","year":"2019","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2021.101340_bib138","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1038\/s41586-019-1439-1","article-title":"Regulation of phosphoribosyl ubiquitination by a calmodulin-dependent glutamylase","volume":"572","author":"Gan","year":"2019","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2021.101340_bib139","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1126\/science.aaw7446","article-title":"Bacterial pseudokinase catalyzes protein polyglutamylation to inhibit the SidE-family ubiquitin ligases","volume":"364","author":"Black","year":"2019","journal-title":"Science"},{"key":"10.1016\/j.jbc.2021.101340_bib140","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1038\/s41586-019-1440-8","article-title":"Inhibition of bacterial ubiquitin ligases by SidJ\u2013calmodulin catalysed glutamylation","volume":"572","author":"Bhogaraju","year":"2019","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2021.101340_bib141","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1016\/j.tim.2019.09.001","article-title":"Glutamylation of bacterial ubiquitin ligases by a Legionella pseudokinase","volume":"27","author":"Sulpizio","year":"2019","journal-title":"Trends Microbiol."},{"key":"10.1016\/j.jbc.2021.101340_bib142","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1038\/cr.2016.30","article-title":"Bacteria-host relationship: Ubiquitin ligases as weapons of invasion","volume":"26","author":"Maculins","year":"2016","journal-title":"Cell Res."},{"key":"10.1016\/j.jbc.2021.101340_bib143","article-title":"Tructural and mechanistic basis for protein glutamylation by the kinase fold","author":"Osinski","year":"2021","journal-title":"bioRxiv"},{"key":"10.1016\/j.jbc.2021.101340_bib144","doi-asserted-by":"crossref","first-page":"3916","DOI":"10.3390\/ijms20163916","article-title":"Multitasking Rab proteins in autophagy and membrane trafficking: A focus on Rab33b","volume":"20","author":"Morgan","year":"2019","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2021.101340_bib145","doi-asserted-by":"crossref","first-page":"2031","DOI":"10.1016\/j.celrep.2017.10.088","article-title":"Positive and negative regulation of the master metabolic regulator mTORC1 by two families of Legionella pneumophila effectors","volume":"21","author":"De Leon","year":"2017","journal-title":"Cell Rep."},{"key":"10.1016\/j.jbc.2021.101340_bib146","doi-asserted-by":"crossref","first-page":"893","DOI":"10.15252\/msb.20167381","article-title":"Diverse mechanisms of metaeffector activity in an intracellular bacterial pathogen, Legionella pneumophila","volume":"12","author":"Urbanus","year":"2016","journal-title":"Mol. Syst. Biol."},{"key":"10.1016\/j.jbc.2021.101340_bib147","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1006186","article-title":"A\u00a0Legionella effector disrupts host cytoskeletal structure by cleaving actin","volume":"13","author":"Liu","year":"2017","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2021.101340_bib148","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1016\/S0962-8924(03)00037-0","article-title":"Bacterial virulence factors targeting Rho GTPases: Parasitism or symbiosis?","volume":"13","author":"Boquet","year":"2003","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.jbc.2021.101340_bib149","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1111\/j.1365-2958.2008.06124.x","article-title":"Legionella translocates an E3 ubiquitin ligase that has multiple U-boxes with distinct functions","volume":"67","author":"Kubori","year":"2008","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2021.101340_bib150","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1001216","article-title":"Legionella metaeffector exploits host proteasome to temporally regulate cognate effector","volume":"6","author":"Kubori","year":"2010","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2021.101340_bib151","doi-asserted-by":"crossref","first-page":"1459","DOI":"10.1016\/j.str.2015.05.020","article-title":"Molecular characterization of LubX: Functional divergence of the U-box fold by Legionella pneumophila","volume":"23","author":"Quaile","year":"2015","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2021.101340_bib152","doi-asserted-by":"crossref","first-page":"18745","DOI":"10.1073\/pnas.0609012103","article-title":"A\u00a0Legionella pneumophila-translocated substrate that is required for growth within macrophages and protection from host cell death","volume":"103","author":"Laguna","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2021.101340_bib153","doi-asserted-by":"crossref","first-page":"2223","DOI":"10.1093\/oxfordjournals.hmg.a018913","article-title":"Myotubularin, a phosphatase deficient in myotubular myopathy, acts on phosphatidylinositol 3-kinase and phosphatidylinositol 3-phosphate pathway","volume":"9","author":"Blondeau","year":"2000","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.jbc.2021.101340_bib154","doi-asserted-by":"crossref","first-page":"8910","DOI":"10.1073\/pnas.160255697","article-title":"Myotubularin, a protein tyrosine phosphatase mutated in myotubular myopathy, dephosphorylates the lipid second messenger, phosphatidylinositol 3-phosphate","volume":"97","author":"Taylor","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2021.101340_bib155","doi-asserted-by":"crossref","first-page":"24518","DOI":"10.1074\/jbc.M113.474239","article-title":"Identification and structural characterization of a Legionella phosphoinositide phosphatase","volume":"288","author":"Toulabi","year":"2013","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101340_bib156","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1126\/science.aay8118","article-title":"Dynamic remodeling of host membranes by self-organizing bacterial effectors","volume":"372","author":"Hsieh","year":"2021","journal-title":"Science"},{"key":"10.1016\/j.jbc.2021.101340_bib157","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1128\/IAI.01081-08","article-title":"The PmrA\/PmrB two-component system of Legionella pneumophila is a Global regulator required for intracellular replication within macrophages and protozoa","volume":"77","author":"Al-Khodor","year":"2009","journal-title":"Infect. Immun."},{"key":"10.1016\/j.jbc.2021.101340_bib158","doi-asserted-by":"crossref","first-page":"1508","DOI":"10.1111\/j.1365-2958.2007.05604.x","article-title":"The response regulator PmrA is a major regulator of the icm\/dot type IV secretion system in Legionella pneumophila and Coxiella burnetii","volume":"63","author":"Zusman","year":"2007","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2021.101340_bib159","doi-asserted-by":"crossref","first-page":"1985","DOI":"10.1128\/JB.01493-07","article-title":"The response regulator CpxR directly regulates expression of several Legionella pneumophila icm\/dot components as well as new translocated substrates","volume":"190","author":"Altman","year":"2008","journal-title":"J.\u00a0Bacteriol."},{"key":"10.1016\/j.jbc.2021.101340_bib160","doi-asserted-by":"crossref","first-page":"4908","DOI":"10.1128\/JB.185.16.4908-4919.2003","article-title":"Identification of CpxR as a positive regulator of icm and dot virulence genes of Legionella pneumophila","volume":"185","author":"Gal-Mor","year":"2003","journal-title":"J.\u00a0Bacteriol."},{"key":"10.1016\/j.jbc.2021.101340_bib161","doi-asserted-by":"crossref","first-page":"995","DOI":"10.1111\/j.1365-2958.2009.06705.x","article-title":"The LetA-RsmYZ-CsrA regulatory cascade, together with RpoS and PmrA, post-transcriptionally regulates stationary phase activation of Legionella pneumophila Icm\/Dot effectors","volume":"72","author":"Rasis","year":"2009","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2021.101340_bib162","doi-asserted-by":"crossref","first-page":"e01313","DOI":"10.1128\/mBio.01313-18","article-title":"Evolution of the arsenal of Legionella pneumophila effectors to modulate protist hosts","volume":"9","author":"Best","year":"2018","journal-title":"MBio"},{"key":"10.1016\/j.jbc.2021.101340_bib163","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1038\/ng.3481","article-title":"Genomic analysis of 38 Legionella species identifies large and diverse effector repertoires","volume":"48","author":"Burstein","year":"2016","journal-title":"Nat. Genet."},{"key":"10.1016\/j.jbc.2021.101340_bib164","doi-asserted-by":"crossref","first-page":"208","DOI":"10.3389\/fmicb.2011.00208","article-title":"Comparative and functional genomics of Legionella identified eukaryotic like proteins as key players in host\u2013pathogen interactions","volume":"2","author":"Gomez-Valero","year":"2011","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.jbc.2021.101340_bib165","doi-asserted-by":"crossref","first-page":"2265","DOI":"10.1073\/pnas.1808016116","article-title":"More than 18,000 effectors in the Legionella genus genome provide multiple, independent combinations for replication in human cells","volume":"116","author":"Gomez-Valero","year":"2019","journal-title":"Proc. Natl. Acad. Sci. U. S. A."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925821011467?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925821011467?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T00:02:11Z","timestamp":1758240131000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925821011467"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,12]]},"references-count":165,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2021,12]]}},"alternative-id":["S0021925821011467"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2021.101340","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2021,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The unity of opposites: Strategic interplay between bacterial effectors to regulate cellular homeostasis","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2021.101340","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"101340"}}