The RickA protein of Rickettsia conorii activates the Arp2/3 complex
Actin polymerization, the main driving force for cell locomotion, is also used by the bacteria Listeria and Shigella and vaccinia virus for intracellular and intercellular movements. Seminal studies have shown the key function of the Arp2/3 complex in nucleating actin and generating a branched array...
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| Veröffentlicht in: | Nature 2004-01, Vol.427 (6973), p.457-461 |
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| creator | Cossart, Pascale Gouin, Edith Egile, Coumaran Dehoux, Pierre Villiers, Véronique Adams, Josephine Gertler, Frank Li, Rong |
| description | Actin polymerization, the main driving force for cell locomotion, is also used by the bacteria Listeria and Shigella and vaccinia virus for intracellular and intercellular movements. Seminal studies have shown the key function of the Arp2/3 complex in nucleating actin and generating a branched array of actin filaments during membrane extension and pathogen movement. Arp2/3 requires activation by proteins such as the WASP-family proteins or ActA of Listeria. We previously reported that actin tails of Rickettsia conorii, another intracellular bacterium, unlike those of Listeria, Shigella or vaccinia, are made of long unbranched actin filaments apparently devoid of Arp2/3 (ref. 4). Here we identify a R. conorii surface protein, RickA, that activates Arp2/3 in vitro, although less efficiently than ActA. In infected cells, Arp2/3 is detected on the rickettsial surface but not in actin tails. When expressed in mammalian cells and targeted to the membrane, RickA induces filopodia. Thus RickA-induced actin polymerization, by generating long actin filaments reminiscent of those present in filopodia, has potential as a tool for studying filopodia formation. |
| doi_str_mv | 10.1038/nature02318 |
| format | Article |
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Seminal studies have shown the key function of the Arp2/3 complex in nucleating actin and generating a branched array of actin filaments during membrane extension and pathogen movement. Arp2/3 requires activation by proteins such as the WASP-family proteins or ActA of Listeria. We previously reported that actin tails of Rickettsia conorii, another intracellular bacterium, unlike those of Listeria, Shigella or vaccinia, are made of long unbranched actin filaments apparently devoid of Arp2/3 (ref. 4). Here we identify a R. conorii surface protein, RickA, that activates Arp2/3 in vitro, although less efficiently than ActA. In infected cells, Arp2/3 is detected on the rickettsial surface but not in actin tails. When expressed in mammalian cells and targeted to the membrane, RickA induces filopodia. Thus RickA-induced actin polymerization, by generating long actin filaments reminiscent of those present in filopodia, has potential as a tool for studying filopodia formation.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/nature02318</identifier><identifier>PMID: 14749835</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Actins - metabolism ; Amino Acid Sequence ; Arp2 protein ; Arp3 protein ; Bacteria ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Bacteriology ; Biological and medical sciences ; Cell adhesion & migration ; Cell Line, Tumor ; Cellular Biology ; Cytoskeletal Proteins - metabolism ; Fundamental and applied biological sciences. Psychology ; Humanities and Social Sciences ; Humans ; letter ; Life Sciences ; Macromolecular Substances ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Microbiology ; Molecular Sequence Data ; multidisciplinary ; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains ; Proteins ; RickA protein ; Rickettsia conorii ; Rickettsia conorii - cytology ; Rickettsia conorii - genetics ; Rickettsia conorii - metabolism ; Science ; Science (multidisciplinary) ; Transfection</subject><ispartof>Nature, 2004-01, Vol.427 (6973), p.457-461</ispartof><rights>Macmillan Magazines Ltd. 2004</rights><rights>2005 INIST-CNRS</rights><rights>COPYRIGHT 2004 Nature Publishing Group</rights><rights>Copyright Macmillan Journals Ltd. 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Thus RickA-induced actin polymerization, by generating long actin filaments reminiscent of those present in filopodia, has potential as a tool for studying filopodia formation.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>14749835</pmid><doi>10.1038/nature02318</doi><tpages>5</tpages><orcidid>https://orcid.org/0000-0001-8871-6780</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0028-0836 |
| ispartof | Nature, 2004-01, Vol.427 (6973), p.457-461 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_hal_primary_oai_HAL_hal_02682797v1 |
| source | MEDLINE; Nature; Alma/SFX Local Collection |
| subjects | Actins - metabolism Amino Acid Sequence Arp2 protein Arp3 protein Bacteria Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacteriology Biological and medical sciences Cell adhesion & migration Cell Line, Tumor Cellular Biology Cytoskeletal Proteins - metabolism Fundamental and applied biological sciences. Psychology Humanities and Social Sciences Humans letter Life Sciences Macromolecular Substances Membrane Proteins - genetics Membrane Proteins - metabolism Microbiology Molecular Sequence Data multidisciplinary Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains Proteins RickA protein Rickettsia conorii Rickettsia conorii - cytology Rickettsia conorii - genetics Rickettsia conorii - metabolism Science Science (multidisciplinary) Transfection |
| title | The RickA protein of Rickettsia conorii activates the Arp2/3 complex |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-27T21%3A08%3A27IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_hal_p&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20RickA%20protein%20of%20Rickettsia%20conorii%20activates%20the%20Arp2/3%20complex&rft.jtitle=Nature&rft.au=Cossart,%20Pascale&rft.date=2004-01-29&rft.volume=427&rft.issue=6973&rft.spage=457&rft.epage=461&rft.pages=457-461&rft.issn=0028-0836&rft.eissn=1476-4687&rft.coden=NATUAS&rft_id=info:doi/10.1038/nature02318&rft_dat=%3Cgale_hal_p%3EA186371658%3C/gale_hal_p%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=204549495&rft_id=info:pmid/14749835&rft_galeid=A186371658&rfr_iscdi=true |