DOCK2 regulates Rac activation and cytoskeletal reorganization through interaction with ELMO1
Although the migratory property of lymphocytes is critical for protective immunity, tissue infiltration of lymphocytes sometimes causes harmful immune responses. DOCK2 plays a critical role in lymphocyte migration by regulating actin cytoskeleton through Rac activation, yet the mechanism by which DO...
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| Veröffentlicht in: | Blood 2003-10, Vol.102 (8), p.2948-2950 |
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| creator | Sanui, Terukazu Inayoshi, Ayumi Noda, Mayuko Iwata, Eiko Stein, Jens V. Sasazuki, Takehiko Fukui, Yoshinori |
| description | Although the migratory property of lymphocytes is critical for protective immunity, tissue infiltration of lymphocytes sometimes causes harmful immune responses. DOCK2 plays a critical role in lymphocyte migration by regulating actin cytoskeleton through Rac activation, yet the mechanism by which DOCK2 activates Rac remains unknown. We found that DOCK2 associates with engulfment and cell motility (ELMO1) through its Srchomology 3 (SH3) domain. When DOCK2 was expressed in T-hybridoma cells lacking endogenous expression of DOCK2, Rac activation and actin polymerization were induced. However, such responses were not elicited by the DOCK2 mutant lacking the region required for ELMO1 binding. On the other hand, we found that the expression of ELMO1 induces Rac activation in the plasmacytoma cells expressing DOCK2 but not ELMO1. These results indicate that the association of DOCK2 with ELMO1 is critical for DOCK2-mediated Rac activation, thereby suggesting that their association might be a therapeutic target for immunologic disorders caused by lymphocyte infiltration. |
| doi_str_mv | 10.1182/blood-2003-01-0173 |
| format | Article |
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DOCK2 plays a critical role in lymphocyte migration by regulating actin cytoskeleton through Rac activation, yet the mechanism by which DOCK2 activates Rac remains unknown. We found that DOCK2 associates with engulfment and cell motility (ELMO1) through its Srchomology 3 (SH3) domain. When DOCK2 was expressed in T-hybridoma cells lacking endogenous expression of DOCK2, Rac activation and actin polymerization were induced. However, such responses were not elicited by the DOCK2 mutant lacking the region required for ELMO1 binding. On the other hand, we found that the expression of ELMO1 induces Rac activation in the plasmacytoma cells expressing DOCK2 but not ELMO1. These results indicate that the association of DOCK2 with ELMO1 is critical for DOCK2-mediated Rac activation, thereby suggesting that their association might be a therapeutic target for immunologic disorders caused by lymphocyte infiltration.</description><identifier>ISSN: 0006-4971</identifier><identifier>EISSN: 1528-0020</identifier><identifier>DOI: 10.1182/blood-2003-01-0173</identifier><identifier>PMID: 12829596</identifier><language>eng</language><publisher>Washington, DC: Elsevier Inc</publisher><subject>Actins - metabolism ; Adaptor Proteins, Signal Transducing ; Biological and medical sciences ; Carrier Proteins - metabolism ; Cell Line ; Cell Movement ; Cytoskeleton - metabolism ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Genetic Vectors ; GTPase-Activating Proteins ; Guanine Nucleotide Exchange Factors ; Humans ; Immunobiology ; Immunoblotting ; Lymphocytes - cytology ; Lymphoid cells: ontogeny, maturation, markers, receptors, circulation and recirculation ; Microscopy, Fluorescence ; Plasmids - metabolism ; Precipitin Tests ; Protein Binding ; Protein Structure, Tertiary ; rac GTP-Binding Proteins - metabolism ; rac1 GTP-Binding Protein - metabolism ; src Homology Domains ; Transfection</subject><ispartof>Blood, 2003-10, Vol.102 (8), p.2948-2950</ispartof><rights>2003 American Society of Hematology</rights><rights>2004 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c426t-23311799dd0712136ee16fb3c86e47eb9b0d1e7d86bcb1e221dd1ec5f89970f83</citedby><cites>FETCH-LOGICAL-c426t-23311799dd0712136ee16fb3c86e47eb9b0d1e7d86bcb1e221dd1ec5f89970f83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15185459$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12829596$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sanui, Terukazu</creatorcontrib><creatorcontrib>Inayoshi, Ayumi</creatorcontrib><creatorcontrib>Noda, Mayuko</creatorcontrib><creatorcontrib>Iwata, Eiko</creatorcontrib><creatorcontrib>Stein, Jens V.</creatorcontrib><creatorcontrib>Sasazuki, Takehiko</creatorcontrib><creatorcontrib>Fukui, Yoshinori</creatorcontrib><title>DOCK2 regulates Rac activation and cytoskeletal reorganization through interaction with ELMO1</title><title>Blood</title><addtitle>Blood</addtitle><description>Although the migratory property of lymphocytes is critical for protective immunity, tissue infiltration of lymphocytes sometimes causes harmful immune responses. 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These results indicate that the association of DOCK2 with ELMO1 is critical for DOCK2-mediated Rac activation, thereby suggesting that their association might be a therapeutic target for immunologic disorders caused by lymphocyte infiltration.</description><subject>Actins - metabolism</subject><subject>Adaptor Proteins, Signal Transducing</subject><subject>Biological and medical sciences</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Line</subject><subject>Cell Movement</subject><subject>Cytoskeleton - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Genetic Vectors</subject><subject>GTPase-Activating Proteins</subject><subject>Guanine Nucleotide Exchange Factors</subject><subject>Humans</subject><subject>Immunobiology</subject><subject>Immunoblotting</subject><subject>Lymphocytes - cytology</subject><subject>Lymphoid cells: ontogeny, maturation, markers, receptors, circulation and recirculation</subject><subject>Microscopy, Fluorescence</subject><subject>Plasmids - metabolism</subject><subject>Precipitin Tests</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>rac GTP-Binding Proteins - metabolism</subject><subject>rac1 GTP-Binding Protein - metabolism</subject><subject>src Homology Domains</subject><subject>Transfection</subject><issn>0006-4971</issn><issn>1528-0020</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE2LFDEQhoMo7rj6BzxIX_TWWpXudDrgRcb1A0cGRI8S0kn1TLSnsybplfXXm3EG9iYEQqqe9yU8jD1FeInY81fDFIKrOUBTA5Yjm3tshYL3NQCH-2wFAF3dKokX7FFKPwCwbbh4yC6Q91wJ1a3Y97fb9SdeRdotk8mUqi_GVsZmf2OyD3NlZlfZ2xzST5oom6mQIe7M7P-c9nkfw7LbV37OFI-5Mvvt87662nze4mP2YDRToifn-5J9e3f1df2h3mzff1y_2dS25V2uedMgSqWcA4kcm44Iu3FobN9RK2lQAzgk6fpusAMS5-jK24qxV0rC2DeX7MWp9zqGXwulrA8-WZomM1NYkpZCipZDW0B-Am0MKUUa9XX0BxNvNYI-StX_pOqjVA2oj1JL6Nm5fRkO5O4iZ4sFeH4GTLJmGqOZrU93nMBetEIV7vWJo-LixlPUyXqaLTkfyWbtgv_fP_4CYHGVRA</recordid><startdate>20031015</startdate><enddate>20031015</enddate><creator>Sanui, Terukazu</creator><creator>Inayoshi, Ayumi</creator><creator>Noda, Mayuko</creator><creator>Iwata, Eiko</creator><creator>Stein, Jens V.</creator><creator>Sasazuki, Takehiko</creator><creator>Fukui, Yoshinori</creator><general>Elsevier Inc</general><general>The Americain Society of Hematology</general><scope>6I.</scope><scope>AAFTH</scope><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>7X8</scope></search><sort><creationdate>20031015</creationdate><title>DOCK2 regulates Rac activation and cytoskeletal reorganization through interaction with ELMO1</title><author>Sanui, Terukazu ; Inayoshi, Ayumi ; Noda, Mayuko ; Iwata, Eiko ; Stein, Jens V. ; Sasazuki, Takehiko ; Fukui, Yoshinori</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c426t-23311799dd0712136ee16fb3c86e47eb9b0d1e7d86bcb1e221dd1ec5f89970f83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Actins - metabolism</topic><topic>Adaptor Proteins, Signal Transducing</topic><topic>Biological and medical sciences</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Line</topic><topic>Cell Movement</topic><topic>Cytoskeleton - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Genetic Vectors</topic><topic>GTPase-Activating Proteins</topic><topic>Guanine Nucleotide Exchange Factors</topic><topic>Humans</topic><topic>Immunobiology</topic><topic>Immunoblotting</topic><topic>Lymphocytes - cytology</topic><topic>Lymphoid cells: ontogeny, maturation, markers, receptors, circulation and recirculation</topic><topic>Microscopy, Fluorescence</topic><topic>Plasmids - metabolism</topic><topic>Precipitin Tests</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>rac GTP-Binding Proteins - metabolism</topic><topic>rac1 GTP-Binding Protein - metabolism</topic><topic>src Homology Domains</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sanui, Terukazu</creatorcontrib><creatorcontrib>Inayoshi, Ayumi</creatorcontrib><creatorcontrib>Noda, Mayuko</creatorcontrib><creatorcontrib>Iwata, Eiko</creatorcontrib><creatorcontrib>Stein, Jens V.</creatorcontrib><creatorcontrib>Sasazuki, Takehiko</creatorcontrib><creatorcontrib>Fukui, Yoshinori</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>MEDLINE - Academic</collection><jtitle>Blood</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sanui, Terukazu</au><au>Inayoshi, Ayumi</au><au>Noda, Mayuko</au><au>Iwata, Eiko</au><au>Stein, Jens V.</au><au>Sasazuki, Takehiko</au><au>Fukui, Yoshinori</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>DOCK2 regulates Rac activation and cytoskeletal reorganization through interaction with ELMO1</atitle><jtitle>Blood</jtitle><addtitle>Blood</addtitle><date>2003-10-15</date><risdate>2003</risdate><volume>102</volume><issue>8</issue><spage>2948</spage><epage>2950</epage><pages>2948-2950</pages><issn>0006-4971</issn><eissn>1528-0020</eissn><abstract>Although the migratory property of lymphocytes is critical for protective immunity, tissue infiltration of lymphocytes sometimes causes harmful immune responses. DOCK2 plays a critical role in lymphocyte migration by regulating actin cytoskeleton through Rac activation, yet the mechanism by which DOCK2 activates Rac remains unknown. We found that DOCK2 associates with engulfment and cell motility (ELMO1) through its Srchomology 3 (SH3) domain. When DOCK2 was expressed in T-hybridoma cells lacking endogenous expression of DOCK2, Rac activation and actin polymerization were induced. However, such responses were not elicited by the DOCK2 mutant lacking the region required for ELMO1 binding. On the other hand, we found that the expression of ELMO1 induces Rac activation in the plasmacytoma cells expressing DOCK2 but not ELMO1. 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| subjects | Actins - metabolism Adaptor Proteins, Signal Transducing Biological and medical sciences Carrier Proteins - metabolism Cell Line Cell Movement Cytoskeleton - metabolism Fundamental and applied biological sciences. Psychology Fundamental immunology Genetic Vectors GTPase-Activating Proteins Guanine Nucleotide Exchange Factors Humans Immunobiology Immunoblotting Lymphocytes - cytology Lymphoid cells: ontogeny, maturation, markers, receptors, circulation and recirculation Microscopy, Fluorescence Plasmids - metabolism Precipitin Tests Protein Binding Protein Structure, Tertiary rac GTP-Binding Proteins - metabolism rac1 GTP-Binding Protein - metabolism src Homology Domains Transfection |
| title | DOCK2 regulates Rac activation and cytoskeletal reorganization through interaction with ELMO1 |
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