The Entamoeba histolytica, Arp2/3 Complex Is Recruited to Phagocytic Cups through an Atypical Kinase EhAK1
The parasite Entamoeba histolytica is the etiological agent of amoebiasis and phagocytosis plays a key role in virulence of this organism. Signaling pathways involved in activation of cytoskeletal dynamics required for phagocytosis remain to be elucidated. Phagocytosis is initiated with sequential r...
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| creator | Babuta, Mrigya Mansuri, M Shahid Bhattacharya, Sudha Bhattacharya, Alok |
| description | The parasite Entamoeba histolytica is the etiological agent of amoebiasis and phagocytosis plays a key role in virulence of this organism. Signaling pathways involved in activation of cytoskeletal dynamics required for phagocytosis remain to be elucidated. Phagocytosis is initiated with sequential recruitment of EhC2PK, EhCaBP1, EhCaBP3 and an atypical kinase EhAK1 after particle attachment. Here we show that EhARPC1, an essential subunit of the actin branching complex Arp 2/3 is recruited to the phagocytic initiation sites by EhAK1. Imaging, expression knockdown of different molecules and pull down experiments suggest that EhARPC1 interacts with EhAK1 and that it is required during initiation of phagocytosis and phagosome formation. Moreover, recruitment of EhARPC2 at the phagocytosis initiation by EhAK1 is also observed, indicating that the Arp 2/3 complex is recruited. In conclusion, these results suggests a novel mechanism of recruitment of Arp 2/3 complex during phagocytosis in E. histolytica. |
| doi_str_mv | 10.1371/journal.ppat.1005310 |
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Signaling pathways involved in activation of cytoskeletal dynamics required for phagocytosis remain to be elucidated. Phagocytosis is initiated with sequential recruitment of EhC2PK, EhCaBP1, EhCaBP3 and an atypical kinase EhAK1 after particle attachment. Here we show that EhARPC1, an essential subunit of the actin branching complex Arp 2/3 is recruited to the phagocytic initiation sites by EhAK1. Imaging, expression knockdown of different molecules and pull down experiments suggest that EhARPC1 interacts with EhAK1 and that it is required during initiation of phagocytosis and phagosome formation. Moreover, recruitment of EhARPC2 at the phagocytosis initiation by EhAK1 is also observed, indicating that the Arp 2/3 complex is recruited. In conclusion, these results suggests a novel mechanism of recruitment of Arp 2/3 complex during phagocytosis in E. histolytica.</description><identifier>ISSN: 1553-7374</identifier><identifier>ISSN: 1553-7366</identifier><identifier>EISSN: 1553-7374</identifier><identifier>DOI: 10.1371/journal.ppat.1005310</identifier><identifier>PMID: 26646565</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Actin-Related Protein 2-3 Complex - metabolism ; Actins - metabolism ; Amebiasis ; Animals ; Blotting, Western ; Cell adhesion & migration ; Cytoskeleton ; Cytoskeleton - metabolism ; Developing countries ; Entamoeba histolytica ; Entamoeba histolytica - metabolism ; Entamoebiasis - metabolism ; Erythrocytes - parasitology ; Experiments ; Fluorescent Antibody Technique ; Immunoprecipitation ; Kinases ; LDCs ; Mice ; Microbiological research ; Motility ; Parasites ; Phagocytosis ; Phagocytosis - physiology ; Physiological aspects ; Polymerase Chain Reaction ; Protein Kinases - metabolism ; Proteins ; Protozoan Proteins - metabolism ; Rabbits ; Recruitment ; Scholarships & fellowships ; Signal Transduction - physiology</subject><ispartof>PLoS pathogens, 2015-12, Vol.11 (12), p.e1005310-e1005310</ispartof><rights>COPYRIGHT 2015 Public Library of Science</rights><rights>2015 Babuta et al 2015 Babuta et al</rights><rights>2015 Public Library of Science. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: , Arp2/3 Complex Is Recruited to Phagocytic Cups through an Atypical Kinase EhAK1. 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Signaling pathways involved in activation of cytoskeletal dynamics required for phagocytosis remain to be elucidated. Phagocytosis is initiated with sequential recruitment of EhC2PK, EhCaBP1, EhCaBP3 and an atypical kinase EhAK1 after particle attachment. Here we show that EhARPC1, an essential subunit of the actin branching complex Arp 2/3 is recruited to the phagocytic initiation sites by EhAK1. Imaging, expression knockdown of different molecules and pull down experiments suggest that EhARPC1 interacts with EhAK1 and that it is required during initiation of phagocytosis and phagosome formation. Moreover, recruitment of EhARPC2 at the phagocytosis initiation by EhAK1 is also observed, indicating that the Arp 2/3 complex is recruited. In conclusion, these results suggests a novel mechanism of recruitment of Arp 2/3 complex during phagocytosis in E. histolytica.</description><subject>Actin-Related Protein 2-3 Complex - metabolism</subject><subject>Actins - metabolism</subject><subject>Amebiasis</subject><subject>Animals</subject><subject>Blotting, Western</subject><subject>Cell adhesion & migration</subject><subject>Cytoskeleton</subject><subject>Cytoskeleton - metabolism</subject><subject>Developing countries</subject><subject>Entamoeba histolytica</subject><subject>Entamoeba histolytica - metabolism</subject><subject>Entamoebiasis - metabolism</subject><subject>Erythrocytes - parasitology</subject><subject>Experiments</subject><subject>Fluorescent Antibody Technique</subject><subject>Immunoprecipitation</subject><subject>Kinases</subject><subject>LDCs</subject><subject>Mice</subject><subject>Microbiological research</subject><subject>Motility</subject><subject>Parasites</subject><subject>Phagocytosis</subject><subject>Phagocytosis - physiology</subject><subject>Physiological aspects</subject><subject>Polymerase Chain Reaction</subject><subject>Protein Kinases - metabolism</subject><subject>Proteins</subject><subject>Protozoan Proteins - metabolism</subject><subject>Rabbits</subject><subject>Recruitment</subject><subject>Scholarships & fellowships</subject><subject>Signal Transduction - physiology</subject><issn>1553-7374</issn><issn>1553-7366</issn><issn>1553-7374</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>DOA</sourceid><recordid>eNqVkl1v0zAUhiMEYlvhHyCwxA1ItIvjjyQ3SFU1oNoEaIxr68Q5-aiSOLMdtP77ubSbVokb5Ivjj-d9j318ougNjReUpfR8YyY7QLcYR_ALGseC0fhZdEqFYPOUpfz5k_lJdObcJo45ZVS-jE4SKbkUUpxGm5sGycXgoTdYAGla50239a2GT2Rpx-SckZXpxw7vyNqRa9R2aj2WxBvys4Ha6B1LVtPoiG-smeqGwECWfjsGi45ctgO4kKBZXtJX0YsKOoevD3EW_f5ycbP6Nr_68XW9Wl7NtcxzPxdFnkiOPBVFkVEGAuMq41khUy2SsEiBlTynSYYgMtBFVeU6xkQiS7Ks4shm0bu979gZpw5lcoqmKcski0OYRes9URrYqNG2PditMtCqvxvG1gpseFeHKq9kVpQFCADKqzChmAtWSEETSeOSBa_Ph2xT0WOpcfAWuiPT45OhbVRt_igu0ySnPBh8OBhYczuh86pvncaugwHNtLs3T8PXyiQJ6Ps9WkO4WjtUJjjqHa6WXHCeBYgGavEPKowS-1abAas27B8JPh4JAuPxztcwOafWv67_g_1-zPI9q61xzmL1WBUaq10PP3yO2vWwOvRwkL19WtFH0UPTsnthcexr</recordid><startdate>20151201</startdate><enddate>20151201</enddate><creator>Babuta, Mrigya</creator><creator>Mansuri, M Shahid</creator><creator>Bhattacharya, Sudha</creator><creator>Bhattacharya, Alok</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>ISN</scope><scope>ISR</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20151201</creationdate><title>The Entamoeba histolytica, Arp2/3 Complex Is Recruited to Phagocytic Cups through an Atypical Kinase EhAK1</title><author>Babuta, Mrigya ; Mansuri, M Shahid ; Bhattacharya, Sudha ; Bhattacharya, Alok</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c699t-5b9264e475bb813a5e0f848b67c525e07a3d49128ea58acbff9c0e26e3288f4e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Actin-Related Protein 2-3 Complex - metabolism</topic><topic>Actins - metabolism</topic><topic>Amebiasis</topic><topic>Animals</topic><topic>Blotting, Western</topic><topic>Cell adhesion & migration</topic><topic>Cytoskeleton</topic><topic>Cytoskeleton - metabolism</topic><topic>Developing countries</topic><topic>Entamoeba histolytica</topic><topic>Entamoeba histolytica - metabolism</topic><topic>Entamoebiasis - metabolism</topic><topic>Erythrocytes - parasitology</topic><topic>Experiments</topic><topic>Fluorescent Antibody Technique</topic><topic>Immunoprecipitation</topic><topic>Kinases</topic><topic>LDCs</topic><topic>Mice</topic><topic>Microbiological research</topic><topic>Motility</topic><topic>Parasites</topic><topic>Phagocytosis</topic><topic>Phagocytosis - physiology</topic><topic>Physiological aspects</topic><topic>Polymerase Chain Reaction</topic><topic>Protein Kinases - metabolism</topic><topic>Proteins</topic><topic>Protozoan Proteins - metabolism</topic><topic>Rabbits</topic><topic>Recruitment</topic><topic>Scholarships & fellowships</topic><topic>Signal Transduction - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Babuta, Mrigya</creatorcontrib><creatorcontrib>Mansuri, M Shahid</creatorcontrib><creatorcontrib>Bhattacharya, Sudha</creatorcontrib><creatorcontrib>Bhattacharya, Alok</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Canada</collection><collection>Gale In Context: Science</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PLoS pathogens</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Babuta, Mrigya</au><au>Mansuri, M Shahid</au><au>Bhattacharya, Sudha</au><au>Bhattacharya, Alok</au><au>Petri, William A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Entamoeba histolytica, Arp2/3 Complex Is Recruited to Phagocytic Cups through an Atypical Kinase EhAK1</atitle><jtitle>PLoS pathogens</jtitle><addtitle>PLoS Pathog</addtitle><date>2015-12-01</date><risdate>2015</risdate><volume>11</volume><issue>12</issue><spage>e1005310</spage><epage>e1005310</epage><pages>e1005310-e1005310</pages><issn>1553-7374</issn><issn>1553-7366</issn><eissn>1553-7374</eissn><abstract>The parasite Entamoeba histolytica is the etiological agent of amoebiasis and phagocytosis plays a key role in virulence of this organism. Signaling pathways involved in activation of cytoskeletal dynamics required for phagocytosis remain to be elucidated. Phagocytosis is initiated with sequential recruitment of EhC2PK, EhCaBP1, EhCaBP3 and an atypical kinase EhAK1 after particle attachment. Here we show that EhARPC1, an essential subunit of the actin branching complex Arp 2/3 is recruited to the phagocytic initiation sites by EhAK1. Imaging, expression knockdown of different molecules and pull down experiments suggest that EhARPC1 interacts with EhAK1 and that it is required during initiation of phagocytosis and phagosome formation. Moreover, recruitment of EhARPC2 at the phagocytosis initiation by EhAK1 is also observed, indicating that the Arp 2/3 complex is recruited. In conclusion, these results suggests a novel mechanism of recruitment of Arp 2/3 complex during phagocytosis in E. histolytica.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>26646565</pmid><doi>10.1371/journal.ppat.1005310</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Actin-Related Protein 2-3 Complex - metabolism Actins - metabolism Amebiasis Animals Blotting, Western Cell adhesion & migration Cytoskeleton Cytoskeleton - metabolism Developing countries Entamoeba histolytica Entamoeba histolytica - metabolism Entamoebiasis - metabolism Erythrocytes - parasitology Experiments Fluorescent Antibody Technique Immunoprecipitation Kinases LDCs Mice Microbiological research Motility Parasites Phagocytosis Phagocytosis - physiology Physiological aspects Polymerase Chain Reaction Protein Kinases - metabolism Proteins Protozoan Proteins - metabolism Rabbits Recruitment Scholarships & fellowships Signal Transduction - physiology |
| title | The Entamoeba histolytica, Arp2/3 Complex Is Recruited to Phagocytic Cups through an Atypical Kinase EhAK1 |
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