ER remodeling by the large GTPase atlastin promotes vacuolar growth of Legionella pneumophila
The pathogenic bacterium Legionella pneumophila replicates in host cells within a distinct ER‐associated compartment termed the Legionella ‐containing vacuole (LCV). How the dynamic ER network contributes to pathogen proliferation within the nascent LCV remains elusive. A proteomic analysis of purif...
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| description | The pathogenic bacterium
Legionella pneumophila
replicates in host cells within a distinct ER‐associated compartment termed the
Legionella
‐containing vacuole (LCV). How the dynamic ER network contributes to pathogen proliferation within the nascent LCV remains elusive. A proteomic analysis of purified LCVs identified the ER tubule‐resident large GTPase atlastin3 (Atl3, yeast Sey1p) and the reticulon protein Rtn4 as conserved LCV host components. Here, we report that Sey1/Atl3 and Rtn4 localize to early LCVs and are critical for pathogen vacuole formation. Sey1 overproduction promotes intracellular growth of
L. pneumophila
, whereas a catalytically inactive, dominant‐negative GTPase mutant protein, or Atl3 depletion, restricts pathogen replication and impairs LCV maturation. Sey1 is not required for initial recruitment of ER to PtdIns(4)
P
‐positive LCVs but for subsequent pathogen vacuole expansion. GTP (but not GDP) catalyzes the Sey1‐dependent aggregation of purified, ER‐positive LCVs
in vitro
. Thus, Sey1/Atl3‐dependent ER remodeling contributes to LCV maturation and intracellular replication of
L. pneumophila
.
Synopsis
The intracellular pathogen
Legionella pneumophila
replicates within a distinct ER‐associated compartment, the
Legionella
‐containing vacuole (LCV). The large, dynamin‐like GTPase atlastin3/Sey1 contributes to LCV maturation and growth by promoting ER tubule dynamics and organelle remodeling.
The ER tubule‐resident large GTPase Atlastin3/Sey1 localizes to LCVs and enhances intracellular replication of
L. pneumophila
.
Sey1 is dispensable for initial recruitment of ER to PtdIns(4)
P
‐positive LCVs but promotes subsequent pathogen vacuole expansion.
GTP (but not GDP) triggers the Sey1‐dependent aggregation of purified, ER‐positive LCVs
in vitro
.
Graphical Abstract
The intracellular pathogen
Legionella pneumophila
replicates within a distinct ER‐associated compartment, the
Legionella
‐containing vacuole (LCV). The large, dynamin‐like GTPase atlastin3/Sey1 contributes to LCV maturation and growth by promoting ER tubule dynamics and organelle remodeling. |
| doi_str_mv | 10.15252/embr.201743903 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_C6C</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5623866</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1932164608</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5133-3e3d066446be2f832719fa6956ced8666ff6e9b4eda2260b4919cf8bd4c847813</originalsourceid><addsrcrecordid>eNqFkc9rFDEcxQdRbK2evUnAi5dt83sSD4KWbSusKKWCFwmZme_MTskkYzLTsv-9qbsuqyCeEsjnvbzHK4qXBJ8SQQU9g6GKpxSTkjON2aPimHCpF4yU6vHuTin5dlQ8S-kWYyx0qZ4WR1QpJgSXx8X35TWKMIQGXO87VG3QtAbkbOwAXd58sQmQnZxNU-_RGMMQJkjoztZzyAzqYrif1ii0aAVdHzw4Z9HoYR7CuO6dfV48aa1L8GJ3nhRfL5Y351eL1efLj-fvV4taEMYWDFiDpeRcVkBbxWhJdGulFrKGRkkp21aCrjg0llKJK66JrltVNbxWvFSEnRTvtr7jXA3Q1OCnaJ0ZYz_YuDHB9ubPF9-vTRfujJCU5Q-ywZudQQw_ZkiTGfpUP9TxEOZkiGaUSC6xyujrv9DbMEef62WKC8wYwzxTZ1uqjiGlCO0-DMHm13TmYTqzny4rXh122PO_t8rA2y1w3zvY_M_PLD99uD50x1txyjrfQTxI_Y9APwHOZrbg</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1945033304</pqid></control><display><type>article</type><title>ER remodeling by the large GTPase atlastin promotes vacuolar growth of Legionella pneumophila</title><source>Springer Nature OA Free Journals</source><creator>Steiner, Bernhard ; Swart, Anna Leoni ; Welin, Amanda ; Weber, Stephen ; Personnic, Nicolas ; Kaech, Andres ; Freyre, Christophe ; Ziegler, Urs ; Klemm, Robin W ; Hilbi, Hubert</creator><creatorcontrib>Steiner, Bernhard ; Swart, Anna Leoni ; Welin, Amanda ; Weber, Stephen ; Personnic, Nicolas ; Kaech, Andres ; Freyre, Christophe ; Ziegler, Urs ; Klemm, Robin W ; Hilbi, Hubert</creatorcontrib><description>The pathogenic bacterium
Legionella pneumophila
replicates in host cells within a distinct ER‐associated compartment termed the
Legionella
‐containing vacuole (LCV). How the dynamic ER network contributes to pathogen proliferation within the nascent LCV remains elusive. A proteomic analysis of purified LCVs identified the ER tubule‐resident large GTPase atlastin3 (Atl3, yeast Sey1p) and the reticulon protein Rtn4 as conserved LCV host components. Here, we report that Sey1/Atl3 and Rtn4 localize to early LCVs and are critical for pathogen vacuole formation. Sey1 overproduction promotes intracellular growth of
L. pneumophila
, whereas a catalytically inactive, dominant‐negative GTPase mutant protein, or Atl3 depletion, restricts pathogen replication and impairs LCV maturation. Sey1 is not required for initial recruitment of ER to PtdIns(4)
P
‐positive LCVs but for subsequent pathogen vacuole expansion. GTP (but not GDP) catalyzes the Sey1‐dependent aggregation of purified, ER‐positive LCVs
in vitro
. Thus, Sey1/Atl3‐dependent ER remodeling contributes to LCV maturation and intracellular replication of
L. pneumophila
.
Synopsis
The intracellular pathogen
Legionella pneumophila
replicates within a distinct ER‐associated compartment, the
Legionella
‐containing vacuole (LCV). The large, dynamin‐like GTPase atlastin3/Sey1 contributes to LCV maturation and growth by promoting ER tubule dynamics and organelle remodeling.
The ER tubule‐resident large GTPase Atlastin3/Sey1 localizes to LCVs and enhances intracellular replication of
L. pneumophila
.
Sey1 is dispensable for initial recruitment of ER to PtdIns(4)
P
‐positive LCVs but promotes subsequent pathogen vacuole expansion.
GTP (but not GDP) triggers the Sey1‐dependent aggregation of purified, ER‐positive LCVs
in vitro
.
Graphical Abstract
The intracellular pathogen
Legionella pneumophila
replicates within a distinct ER‐associated compartment, the
Legionella
‐containing vacuole (LCV). The large, dynamin‐like GTPase atlastin3/Sey1 contributes to LCV maturation and growth by promoting ER tubule dynamics and organelle remodeling.</description><identifier>ISSN: 1469-221X</identifier><identifier>EISSN: 1469-3178</identifier><identifier>DOI: 10.15252/embr.201743903</identifier><identifier>PMID: 28835546</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>A549 Cells ; Agglomeration ; Dictyostelium - microbiology ; Dictyostelium discoideum ; Dynamin ; EMBO20 ; EMBO23 ; Endoplasmic reticulum ; Endoplasmic Reticulum - microbiology ; Endoplasmic Reticulum - physiology ; GTP-Binding Proteins - genetics ; GTP-Binding Proteins - metabolism ; Guanosine triphosphatases ; Guanosine triphosphate ; Humans ; Intracellular ; Legionella ; Legionella pneumophila - growth & development ; Legionella pneumophila - pathogenicity ; Legionnaires' disease bacterium ; macrophage ; Macrophages - microbiology ; Maturation ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Nogo Proteins - genetics ; Nogo Proteins - metabolism ; pathogen vacuole ; Pathogens ; phosphoinositide lipid ; Proteomics ; Recruitment ; Replication ; type IV secretion ; Type IV Secretion Systems ; Vacuoles - metabolism ; Vacuoles - microbiology ; Yeast ; Yeasts</subject><ispartof>EMBO reports, 2017-10, Vol.18 (10), p.1817-1836</ispartof><rights>The Authors 2017</rights><rights>2017 The Authors</rights><rights>2017 The Authors.</rights><rights>2017 EMBO</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5133-3e3d066446be2f832719fa6956ced8666ff6e9b4eda2260b4919cf8bd4c847813</citedby><cites>FETCH-LOGICAL-c5133-3e3d066446be2f832719fa6956ced8666ff6e9b4eda2260b4919cf8bd4c847813</cites><orcidid>0000-0001-8460-5952 ; 0000-0002-5462-9301</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5623866/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5623866/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,41120,42189,45574,45575,46409,46833,51576,53791,53793</link.rule.ids><linktorsrc>$$Uhttps://doi.org/10.15252/embr.201743903$$EView_record_in_Springer_Nature$$FView_record_in_$$GSpringer_Nature</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28835546$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Steiner, Bernhard</creatorcontrib><creatorcontrib>Swart, Anna Leoni</creatorcontrib><creatorcontrib>Welin, Amanda</creatorcontrib><creatorcontrib>Weber, Stephen</creatorcontrib><creatorcontrib>Personnic, Nicolas</creatorcontrib><creatorcontrib>Kaech, Andres</creatorcontrib><creatorcontrib>Freyre, Christophe</creatorcontrib><creatorcontrib>Ziegler, Urs</creatorcontrib><creatorcontrib>Klemm, Robin W</creatorcontrib><creatorcontrib>Hilbi, Hubert</creatorcontrib><title>ER remodeling by the large GTPase atlastin promotes vacuolar growth of Legionella pneumophila</title><title>EMBO reports</title><addtitle>EMBO Rep</addtitle><addtitle>EMBO Rep</addtitle><description>The pathogenic bacterium
Legionella pneumophila
replicates in host cells within a distinct ER‐associated compartment termed the
Legionella
‐containing vacuole (LCV). How the dynamic ER network contributes to pathogen proliferation within the nascent LCV remains elusive. A proteomic analysis of purified LCVs identified the ER tubule‐resident large GTPase atlastin3 (Atl3, yeast Sey1p) and the reticulon protein Rtn4 as conserved LCV host components. Here, we report that Sey1/Atl3 and Rtn4 localize to early LCVs and are critical for pathogen vacuole formation. Sey1 overproduction promotes intracellular growth of
L. pneumophila
, whereas a catalytically inactive, dominant‐negative GTPase mutant protein, or Atl3 depletion, restricts pathogen replication and impairs LCV maturation. Sey1 is not required for initial recruitment of ER to PtdIns(4)
P
‐positive LCVs but for subsequent pathogen vacuole expansion. GTP (but not GDP) catalyzes the Sey1‐dependent aggregation of purified, ER‐positive LCVs
in vitro
. Thus, Sey1/Atl3‐dependent ER remodeling contributes to LCV maturation and intracellular replication of
L. pneumophila
.
Synopsis
The intracellular pathogen
Legionella pneumophila
replicates within a distinct ER‐associated compartment, the
Legionella
‐containing vacuole (LCV). The large, dynamin‐like GTPase atlastin3/Sey1 contributes to LCV maturation and growth by promoting ER tubule dynamics and organelle remodeling.
The ER tubule‐resident large GTPase Atlastin3/Sey1 localizes to LCVs and enhances intracellular replication of
L. pneumophila
.
Sey1 is dispensable for initial recruitment of ER to PtdIns(4)
P
‐positive LCVs but promotes subsequent pathogen vacuole expansion.
GTP (but not GDP) triggers the Sey1‐dependent aggregation of purified, ER‐positive LCVs
in vitro
.
Graphical Abstract
The intracellular pathogen
Legionella pneumophila
replicates within a distinct ER‐associated compartment, the
Legionella
‐containing vacuole (LCV). The large, dynamin‐like GTPase atlastin3/Sey1 contributes to LCV maturation and growth by promoting ER tubule dynamics and organelle remodeling.</description><subject>A549 Cells</subject><subject>Agglomeration</subject><subject>Dictyostelium - microbiology</subject><subject>Dictyostelium discoideum</subject><subject>Dynamin</subject><subject>EMBO20</subject><subject>EMBO23</subject><subject>Endoplasmic reticulum</subject><subject>Endoplasmic Reticulum - microbiology</subject><subject>Endoplasmic Reticulum - physiology</subject><subject>GTP-Binding Proteins - genetics</subject><subject>GTP-Binding Proteins - metabolism</subject><subject>Guanosine triphosphatases</subject><subject>Guanosine triphosphate</subject><subject>Humans</subject><subject>Intracellular</subject><subject>Legionella</subject><subject>Legionella pneumophila - growth & development</subject><subject>Legionella pneumophila - pathogenicity</subject><subject>Legionnaires' disease bacterium</subject><subject>macrophage</subject><subject>Macrophages - microbiology</subject><subject>Maturation</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Nogo Proteins - genetics</subject><subject>Nogo Proteins - metabolism</subject><subject>pathogen vacuole</subject><subject>Pathogens</subject><subject>phosphoinositide lipid</subject><subject>Proteomics</subject><subject>Recruitment</subject><subject>Replication</subject><subject>type IV secretion</subject><subject>Type IV Secretion Systems</subject><subject>Vacuoles - metabolism</subject><subject>Vacuoles - microbiology</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>1469-221X</issn><issn>1469-3178</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9rFDEcxQdRbK2evUnAi5dt83sSD4KWbSusKKWCFwmZme_MTskkYzLTsv-9qbsuqyCeEsjnvbzHK4qXBJ8SQQU9g6GKpxSTkjON2aPimHCpF4yU6vHuTin5dlQ8S-kWYyx0qZ4WR1QpJgSXx8X35TWKMIQGXO87VG3QtAbkbOwAXd58sQmQnZxNU-_RGMMQJkjoztZzyAzqYrif1ii0aAVdHzw4Z9HoYR7CuO6dfV48aa1L8GJ3nhRfL5Y351eL1efLj-fvV4taEMYWDFiDpeRcVkBbxWhJdGulFrKGRkkp21aCrjg0llKJK66JrltVNbxWvFSEnRTvtr7jXA3Q1OCnaJ0ZYz_YuDHB9ubPF9-vTRfujJCU5Q-ywZudQQw_ZkiTGfpUP9TxEOZkiGaUSC6xyujrv9DbMEef62WKC8wYwzxTZ1uqjiGlCO0-DMHm13TmYTqzny4rXh122PO_t8rA2y1w3zvY_M_PLD99uD50x1txyjrfQTxI_Y9APwHOZrbg</recordid><startdate>201710</startdate><enddate>201710</enddate><creator>Steiner, Bernhard</creator><creator>Swart, Anna Leoni</creator><creator>Welin, Amanda</creator><creator>Weber, Stephen</creator><creator>Personnic, Nicolas</creator><creator>Kaech, Andres</creator><creator>Freyre, Christophe</creator><creator>Ziegler, Urs</creator><creator>Klemm, Robin W</creator><creator>Hilbi, Hubert</creator><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>John Wiley and Sons Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7T5</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-8460-5952</orcidid><orcidid>https://orcid.org/0000-0002-5462-9301</orcidid></search><sort><creationdate>201710</creationdate><title>ER remodeling by the large GTPase atlastin promotes vacuolar growth of Legionella pneumophila</title><author>Steiner, Bernhard ; Swart, Anna Leoni ; Welin, Amanda ; Weber, Stephen ; Personnic, Nicolas ; Kaech, Andres ; Freyre, Christophe ; Ziegler, Urs ; Klemm, Robin W ; Hilbi, Hubert</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5133-3e3d066446be2f832719fa6956ced8666ff6e9b4eda2260b4919cf8bd4c847813</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>A549 Cells</topic><topic>Agglomeration</topic><topic>Dictyostelium - microbiology</topic><topic>Dictyostelium discoideum</topic><topic>Dynamin</topic><topic>EMBO20</topic><topic>EMBO23</topic><topic>Endoplasmic reticulum</topic><topic>Endoplasmic Reticulum - microbiology</topic><topic>Endoplasmic Reticulum - physiology</topic><topic>GTP-Binding Proteins - genetics</topic><topic>GTP-Binding Proteins - metabolism</topic><topic>Guanosine triphosphatases</topic><topic>Guanosine triphosphate</topic><topic>Humans</topic><topic>Intracellular</topic><topic>Legionella</topic><topic>Legionella pneumophila - growth & development</topic><topic>Legionella pneumophila - pathogenicity</topic><topic>Legionnaires' disease bacterium</topic><topic>macrophage</topic><topic>Macrophages - microbiology</topic><topic>Maturation</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Nogo Proteins - genetics</topic><topic>Nogo Proteins - metabolism</topic><topic>pathogen vacuole</topic><topic>Pathogens</topic><topic>phosphoinositide lipid</topic><topic>Proteomics</topic><topic>Recruitment</topic><topic>Replication</topic><topic>type IV secretion</topic><topic>Type IV Secretion Systems</topic><topic>Vacuoles - metabolism</topic><topic>Vacuoles - microbiology</topic><topic>Yeast</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Steiner, Bernhard</creatorcontrib><creatorcontrib>Swart, Anna Leoni</creatorcontrib><creatorcontrib>Welin, Amanda</creatorcontrib><creatorcontrib>Weber, Stephen</creatorcontrib><creatorcontrib>Personnic, Nicolas</creatorcontrib><creatorcontrib>Kaech, Andres</creatorcontrib><creatorcontrib>Freyre, Christophe</creatorcontrib><creatorcontrib>Ziegler, Urs</creatorcontrib><creatorcontrib>Klemm, Robin W</creatorcontrib><creatorcontrib>Hilbi, Hubert</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>EMBO reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Steiner, Bernhard</au><au>Swart, Anna Leoni</au><au>Welin, Amanda</au><au>Weber, Stephen</au><au>Personnic, Nicolas</au><au>Kaech, Andres</au><au>Freyre, Christophe</au><au>Ziegler, Urs</au><au>Klemm, Robin W</au><au>Hilbi, Hubert</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>ER remodeling by the large GTPase atlastin promotes vacuolar growth of Legionella pneumophila</atitle><jtitle>EMBO reports</jtitle><stitle>EMBO Rep</stitle><addtitle>EMBO Rep</addtitle><date>2017-10</date><risdate>2017</risdate><volume>18</volume><issue>10</issue><spage>1817</spage><epage>1836</epage><pages>1817-1836</pages><issn>1469-221X</issn><eissn>1469-3178</eissn><abstract>The pathogenic bacterium
Legionella pneumophila
replicates in host cells within a distinct ER‐associated compartment termed the
Legionella
‐containing vacuole (LCV). How the dynamic ER network contributes to pathogen proliferation within the nascent LCV remains elusive. A proteomic analysis of purified LCVs identified the ER tubule‐resident large GTPase atlastin3 (Atl3, yeast Sey1p) and the reticulon protein Rtn4 as conserved LCV host components. Here, we report that Sey1/Atl3 and Rtn4 localize to early LCVs and are critical for pathogen vacuole formation. Sey1 overproduction promotes intracellular growth of
L. pneumophila
, whereas a catalytically inactive, dominant‐negative GTPase mutant protein, or Atl3 depletion, restricts pathogen replication and impairs LCV maturation. Sey1 is not required for initial recruitment of ER to PtdIns(4)
P
‐positive LCVs but for subsequent pathogen vacuole expansion. GTP (but not GDP) catalyzes the Sey1‐dependent aggregation of purified, ER‐positive LCVs
in vitro
. Thus, Sey1/Atl3‐dependent ER remodeling contributes to LCV maturation and intracellular replication of
L. pneumophila
.
Synopsis
The intracellular pathogen
Legionella pneumophila
replicates within a distinct ER‐associated compartment, the
Legionella
‐containing vacuole (LCV). The large, dynamin‐like GTPase atlastin3/Sey1 contributes to LCV maturation and growth by promoting ER tubule dynamics and organelle remodeling.
The ER tubule‐resident large GTPase Atlastin3/Sey1 localizes to LCVs and enhances intracellular replication of
L. pneumophila
.
Sey1 is dispensable for initial recruitment of ER to PtdIns(4)
P
‐positive LCVs but promotes subsequent pathogen vacuole expansion.
GTP (but not GDP) triggers the Sey1‐dependent aggregation of purified, ER‐positive LCVs
in vitro
.
Graphical Abstract
The intracellular pathogen
Legionella pneumophila
replicates within a distinct ER‐associated compartment, the
Legionella
‐containing vacuole (LCV). The large, dynamin‐like GTPase atlastin3/Sey1 contributes to LCV maturation and growth by promoting ER tubule dynamics and organelle remodeling.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>28835546</pmid><doi>10.15252/embr.201743903</doi><tpages>20</tpages><orcidid>https://orcid.org/0000-0001-8460-5952</orcidid><orcidid>https://orcid.org/0000-0002-5462-9301</orcidid><oa>free_for_read</oa></addata></record> |
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| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5623866 |
| source | Springer Nature OA Free Journals |
| subjects | A549 Cells Agglomeration Dictyostelium - microbiology Dictyostelium discoideum Dynamin EMBO20 EMBO23 Endoplasmic reticulum Endoplasmic Reticulum - microbiology Endoplasmic Reticulum - physiology GTP-Binding Proteins - genetics GTP-Binding Proteins - metabolism Guanosine triphosphatases Guanosine triphosphate Humans Intracellular Legionella Legionella pneumophila - growth & development Legionella pneumophila - pathogenicity Legionnaires' disease bacterium macrophage Macrophages - microbiology Maturation Membrane Proteins - genetics Membrane Proteins - metabolism Nogo Proteins - genetics Nogo Proteins - metabolism pathogen vacuole Pathogens phosphoinositide lipid Proteomics Recruitment Replication type IV secretion Type IV Secretion Systems Vacuoles - metabolism Vacuoles - microbiology Yeast Yeasts |
| title | ER remodeling by the large GTPase atlastin promotes vacuolar growth of Legionella pneumophila |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-23T04%3A23%3A24IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_C6C&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=ER%20remodeling%20by%20the%20large%20GTPase%20atlastin%20promotes%20vacuolar%20growth%20of%20Legionella%20pneumophila&rft.jtitle=EMBO%20reports&rft.au=Steiner,%20Bernhard&rft.date=2017-10&rft.volume=18&rft.issue=10&rft.spage=1817&rft.epage=1836&rft.pages=1817-1836&rft.issn=1469-221X&rft.eissn=1469-3178&rft_id=info:doi/10.15252/embr.201743903&rft_dat=%3Cproquest_C6C%3E1932164608%3C/proquest_C6C%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1945033304&rft_id=info:pmid/28835546&rfr_iscdi=true |