Entamoeba histolytica: Identification of EhGPCR-1, a novel putative G protein-coupled receptor that binds to EhRabB
EhRabB is an Entamoeba histolytica protein involved in phagocytosis. However, proteins that regulate the EhRabB activity are unknown. Here, we report the identification of a putative G protein-coupled receptor of E. histolytica (EhGPCR-1) that binds to EhRabB. By two-hybrid screening, we found a 372...
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| Veröffentlicht in: | Experimental parasitology 2005-07, Vol.110 (3), p.253-258 |
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| creator | Picazarri, Karina Luna-Arias, Juan Pedro Carrillo, Eduardo Orozco, Esther Rodriguez, Mario A. |
| description | EhRabB is an
Entamoeba histolytica protein involved in phagocytosis. However, proteins that regulate the EhRabB activity are unknown. Here, we report the identification of a putative G protein-coupled receptor of
E. histolytica (EhGPCR-1) that binds to EhRabB. By two-hybrid screening, we found a 372-bp
cDNA fragment that encodes the C-terminus of EhGPCR-1. The cloning and sequence of the full-length
cDNA revealed that it predicts a polypeptide with two tyrosine-based sorting signals for endocytosis and seven transmembranal domains. These results suggest that EhGPCR-1 could be a GPCR involved in phagocytosis. EhGPCR-1 could be a member of the Rhodopsin family, characterized by a short N-terminus without cysteine residues. |
| doi_str_mv | 10.1016/j.exppara.2005.02.014 |
| format | Article |
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Entamoeba histolytica protein involved in phagocytosis. However, proteins that regulate the EhRabB activity are unknown. Here, we report the identification of a putative G protein-coupled receptor of
E. histolytica (EhGPCR-1) that binds to EhRabB. By two-hybrid screening, we found a 372-bp
cDNA fragment that encodes the C-terminus of EhGPCR-1. The cloning and sequence of the full-length
cDNA revealed that it predicts a polypeptide with two tyrosine-based sorting signals for endocytosis and seven transmembranal domains. These results suggest that EhGPCR-1 could be a GPCR involved in phagocytosis. EhGPCR-1 could be a member of the Rhodopsin family, characterized by a short N-terminus without cysteine residues.</description><identifier>ISSN: 0014-4894</identifier><identifier>EISSN: 1090-2449</identifier><identifier>DOI: 10.1016/j.exppara.2005.02.014</identifier><identifier>PMID: 15955320</identifier><identifier>CODEN: EXPAAA</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Biological and medical sciences ; DNA, Complementary - chemistry ; DNA, Complementary - isolation & purification ; EhRabB ; Entamoeba histolytica ; Entamoeba histolytica - genetics ; Entamoeba histolytica - immunology ; Entamoeba histolytica - metabolism ; Fundamental and applied biological sciences. Psychology ; G protein-coupled receptors ; GDI ; GDP-dissociation inhibitor ; GEF ; GPCRs ; guanine exchange factor ; Life cycle. Host-agent relationship. Pathogenesis ; Molecular Sequence Data ; open reading frame ; ORF ; Phagocytosis ; Phagocytosis - physiology ; Phylogeny ; Protozoa ; rab GTP-Binding Proteins - metabolism ; Rab GTPase ; Receptors, G-Protein-Coupled - chemistry ; Receptors, G-Protein-Coupled - genetics ; Receptors, G-Protein-Coupled - metabolism ; Sequence Alignment ; synthetic dropout medium ; transmembranal</subject><ispartof>Experimental parasitology, 2005-07, Vol.110 (3), p.253-258</ispartof><rights>2005 Elsevier Inc.</rights><rights>2005 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c455t-54a8dde7d2f31f0904726fb2b1928f077a89a8d1b0e9cfcc3a12f31c71c0c8aa3</citedby><cites>FETCH-LOGICAL-c455t-54a8dde7d2f31f0904726fb2b1928f077a89a8d1b0e9cfcc3a12f31c71c0c8aa3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.exppara.2005.02.014$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16872279$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15955320$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Picazarri, Karina</creatorcontrib><creatorcontrib>Luna-Arias, Juan Pedro</creatorcontrib><creatorcontrib>Carrillo, Eduardo</creatorcontrib><creatorcontrib>Orozco, Esther</creatorcontrib><creatorcontrib>Rodriguez, Mario A.</creatorcontrib><title>Entamoeba histolytica: Identification of EhGPCR-1, a novel putative G protein-coupled receptor that binds to EhRabB</title><title>Experimental parasitology</title><addtitle>Exp Parasitol</addtitle><description>EhRabB is an
Entamoeba histolytica protein involved in phagocytosis. However, proteins that regulate the EhRabB activity are unknown. Here, we report the identification of a putative G protein-coupled receptor of
E. histolytica (EhGPCR-1) that binds to EhRabB. By two-hybrid screening, we found a 372-bp
cDNA fragment that encodes the C-terminus of EhGPCR-1. The cloning and sequence of the full-length
cDNA revealed that it predicts a polypeptide with two tyrosine-based sorting signals for endocytosis and seven transmembranal domains. These results suggest that EhGPCR-1 could be a GPCR involved in phagocytosis. EhGPCR-1 could be a member of the Rhodopsin family, characterized by a short N-terminus without cysteine residues.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>DNA, Complementary - chemistry</subject><subject>DNA, Complementary - isolation & purification</subject><subject>EhRabB</subject><subject>Entamoeba histolytica</subject><subject>Entamoeba histolytica - genetics</subject><subject>Entamoeba histolytica - immunology</subject><subject>Entamoeba histolytica - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>G protein-coupled receptors</subject><subject>GDI</subject><subject>GDP-dissociation inhibitor</subject><subject>GEF</subject><subject>GPCRs</subject><subject>guanine exchange factor</subject><subject>Life cycle. Host-agent relationship. Pathogenesis</subject><subject>Molecular Sequence Data</subject><subject>open reading frame</subject><subject>ORF</subject><subject>Phagocytosis</subject><subject>Phagocytosis - physiology</subject><subject>Phylogeny</subject><subject>Protozoa</subject><subject>rab GTP-Binding Proteins - metabolism</subject><subject>Rab GTPase</subject><subject>Receptors, G-Protein-Coupled - chemistry</subject><subject>Receptors, G-Protein-Coupled - genetics</subject><subject>Receptors, G-Protein-Coupled - metabolism</subject><subject>Sequence Alignment</subject><subject>synthetic dropout medium</subject><subject>transmembranal</subject><issn>0014-4894</issn><issn>1090-2449</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU2P0zAQQC0EYruFnwDyBU4kjB07H1wQVN2y0kqgFZwtx5mortI42E7F_ntcNdIeexpr_GY840fIOwY5A1Z-PuT4b5q01zkHkDnwHJh4QVYMGsi4EM1LsoKUykTdiBtyG8IBAGrGxWtyw2QjZcFhRcJ2jProsNV0b0N0w1O0Rn-h9x2O0fbpHK0bqevpdr_7tXnM2Ceq6ehOONBpjun2hHRHJ-8i2jEzbp4G7KhHg1N0nsa9jrS1YxdodKnHo26_vyGvej0EfLvENflzt_29-ZE9_Nzdb749ZEZIGTMpdN11WHW8L1if1hIVL_uWt6zhdQ9VpesmEawFbExvTKHZmTQVM2BqrYs1-Xjpm6b7O2OI6miDwWHQI7o5qLJqCilleRXk0EhWi-oqyCoJBQiZQHkBjXcheOzV5O1R-yfFQJ39qYNa_KmzPwVcJVmp7v3ywNwesXuuWoQl4MMC6GD00Hs9GhueubKuOE97rcnXC4fpg08WvQrG4miws8lNVJ2zV0b5D5Xou5A</recordid><startdate>20050701</startdate><enddate>20050701</enddate><creator>Picazarri, Karina</creator><creator>Luna-Arias, Juan Pedro</creator><creator>Carrillo, Eduardo</creator><creator>Orozco, Esther</creator><creator>Rodriguez, Mario A.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</scope><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>M7N</scope><scope>C1K</scope><scope>F1W</scope><scope>H95</scope><scope>H97</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>20050701</creationdate><title>Entamoeba histolytica: Identification of EhGPCR-1, a novel putative G protein-coupled receptor that binds to EhRabB</title><author>Picazarri, Karina ; Luna-Arias, Juan Pedro ; Carrillo, Eduardo ; Orozco, Esther ; Rodriguez, Mario A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c455t-54a8dde7d2f31f0904726fb2b1928f077a89a8d1b0e9cfcc3a12f31c71c0c8aa3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>DNA, Complementary - chemistry</topic><topic>DNA, Complementary - isolation & purification</topic><topic>EhRabB</topic><topic>Entamoeba histolytica</topic><topic>Entamoeba histolytica - genetics</topic><topic>Entamoeba histolytica - immunology</topic><topic>Entamoeba histolytica - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>G protein-coupled receptors</topic><topic>GDI</topic><topic>GDP-dissociation inhibitor</topic><topic>GEF</topic><topic>GPCRs</topic><topic>guanine exchange factor</topic><topic>Life cycle. Host-agent relationship. Pathogenesis</topic><topic>Molecular Sequence Data</topic><topic>open reading frame</topic><topic>ORF</topic><topic>Phagocytosis</topic><topic>Phagocytosis - physiology</topic><topic>Phylogeny</topic><topic>Protozoa</topic><topic>rab GTP-Binding Proteins - metabolism</topic><topic>Rab GTPase</topic><topic>Receptors, G-Protein-Coupled - chemistry</topic><topic>Receptors, G-Protein-Coupled - genetics</topic><topic>Receptors, G-Protein-Coupled - metabolism</topic><topic>Sequence Alignment</topic><topic>synthetic dropout medium</topic><topic>transmembranal</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Picazarri, Karina</creatorcontrib><creatorcontrib>Luna-Arias, Juan Pedro</creatorcontrib><creatorcontrib>Carrillo, Eduardo</creatorcontrib><creatorcontrib>Orozco, Esther</creatorcontrib><creatorcontrib>Rodriguez, Mario A.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 3: Aquatic Pollution & Environmental Quality</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><jtitle>Experimental parasitology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Picazarri, Karina</au><au>Luna-Arias, Juan Pedro</au><au>Carrillo, Eduardo</au><au>Orozco, Esther</au><au>Rodriguez, Mario A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Entamoeba histolytica: Identification of EhGPCR-1, a novel putative G protein-coupled receptor that binds to EhRabB</atitle><jtitle>Experimental parasitology</jtitle><addtitle>Exp Parasitol</addtitle><date>2005-07-01</date><risdate>2005</risdate><volume>110</volume><issue>3</issue><spage>253</spage><epage>258</epage><pages>253-258</pages><issn>0014-4894</issn><eissn>1090-2449</eissn><coden>EXPAAA</coden><abstract>EhRabB is an
Entamoeba histolytica protein involved in phagocytosis. However, proteins that regulate the EhRabB activity are unknown. Here, we report the identification of a putative G protein-coupled receptor of
E. histolytica (EhGPCR-1) that binds to EhRabB. By two-hybrid screening, we found a 372-bp
cDNA fragment that encodes the C-terminus of EhGPCR-1. The cloning and sequence of the full-length
cDNA revealed that it predicts a polypeptide with two tyrosine-based sorting signals for endocytosis and seven transmembranal domains. These results suggest that EhGPCR-1 could be a GPCR involved in phagocytosis. EhGPCR-1 could be a member of the Rhodopsin family, characterized by a short N-terminus without cysteine residues.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>15955320</pmid><doi>10.1016/j.exppara.2005.02.014</doi><tpages>6</tpages></addata></record> |
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| subjects | Amino Acid Sequence Animals Base Sequence Biological and medical sciences DNA, Complementary - chemistry DNA, Complementary - isolation & purification EhRabB Entamoeba histolytica Entamoeba histolytica - genetics Entamoeba histolytica - immunology Entamoeba histolytica - metabolism Fundamental and applied biological sciences. Psychology G protein-coupled receptors GDI GDP-dissociation inhibitor GEF GPCRs guanine exchange factor Life cycle. Host-agent relationship. Pathogenesis Molecular Sequence Data open reading frame ORF Phagocytosis Phagocytosis - physiology Phylogeny Protozoa rab GTP-Binding Proteins - metabolism Rab GTPase Receptors, G-Protein-Coupled - chemistry Receptors, G-Protein-Coupled - genetics Receptors, G-Protein-Coupled - metabolism Sequence Alignment synthetic dropout medium transmembranal |
| title | Entamoeba histolytica: Identification of EhGPCR-1, a novel putative G protein-coupled receptor that binds to EhRabB |
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