Endocytosis of E-Cadherin Regulated by Rac and Cdc42 Small G Proteins through IQGAP1 and Actin Filaments
E-cadherin is a key cell-cell adhesion molecule at adherens junctions (AJs) and undergoes endocytosis when AJs are disrupted by the action of extracellular signals. To elucidate the mechanism of this endocytosis, we developed here a new cell-free assay system for this reaction using the AJ-enriched...
Gespeichert in:
| Veröffentlicht in: | The Journal of cell biology 2004-07, Vol.166 (2), p.237-248 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 248 |
|---|---|
| container_issue | 2 |
| container_start_page | 237 |
| container_title | The Journal of cell biology |
| container_volume | 166 |
| creator | Izumi, Genkichi Sakisaka, Toshiaki Baba, Takeshi Tanaka, Shintaro Morimoto, Koji Takai, Yoshimi |
| description | E-cadherin is a key cell-cell adhesion molecule at adherens junctions (AJs) and undergoes endocytosis when AJs are disrupted by the action of extracellular signals. To elucidate the mechanism of this endocytosis, we developed here a new cell-free assay system for this reaction using the AJ-enriched fraction from rat liver. We found here that non-trans-interacting, but not trans-interacting, E-cadherin underwent endocytosis in a clathrin-dependent manner. The endocytosis of trans-interacting E-cadherin was inhibited by Rac and Cdc42 small G proteins, which were activated by trans-interacting E-cadherin or trans-interacting nectins, which are known to induce the formation of AJs in cooperation with E-cadherin. This inhibition was mediated by reorganization of the actin cytoskeleton by Rac and Cdc42 through IQGAP1, an actin filament-binding protein and a downstream target of Rac and Cdc42. These results indicate the important role of the Rac/Cdc42-IQGAP1 system in the dynamic organization and maintenance of the E-cadherin-based AJs. |
| doi_str_mv | 10.1083/jcb.200401078 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2172308</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>1622098</jstor_id><sourcerecordid>1622098</sourcerecordid><originalsourceid>FETCH-LOGICAL-c497t-2b73f122cd8c35bed235cf91891b9eedfbe8adfdab2232bdc0041728470dae893</originalsourceid><addsrcrecordid>eNpdkc1v0zAYhy0EYqVw5IaQtQO3DPu1kzgXpKrqyqRJjAFny19pUiXxsB2k_ve4tNqA03t4Hz3vxw-ht5RcUSLYx73RV0AIJ5TU4hla0JKTQlBOnqMFIUCLpoTyAr2KcU8yVnP2El3QEipGaLNA3Way3hySj33EvsWbYq1s50I_4Xu3mweVnMX6gO-VwWqyeG0NB_xtVMOAt_gu-OT6KeLUBT_vOnzzdbu6o3_IlUlZct0PanRTiq_Ri1YN0b051yX6cb35vv5c3H7Z3qxXt4XhTZ0K0DVrKYCxwrBSOwusNG1DRUN145xttRPKtlZpAAbamnwTrUHwmljlRMOW6NPJ-zDr0VmTZwc1yIfQjyocpFe9_Lcz9Z3c-V8Ssobljy7Rh7Mg-J-zi0mOfTRuGNTk_BxlVdVQ1vQ46fI_cO_nMOXjji4iuKh4hooTZIKPMbj2cRNK5DFAmQOUjwFm_v3f6z_R58Qy8O4E7GPy4alfAZBGsN-eTp-R</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>217084864</pqid></control><display><type>article</type><title>Endocytosis of E-Cadherin Regulated by Rac and Cdc42 Small G Proteins through IQGAP1 and Actin Filaments</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Izumi, Genkichi ; Sakisaka, Toshiaki ; Baba, Takeshi ; Tanaka, Shintaro ; Morimoto, Koji ; Takai, Yoshimi</creator><creatorcontrib>Izumi, Genkichi ; Sakisaka, Toshiaki ; Baba, Takeshi ; Tanaka, Shintaro ; Morimoto, Koji ; Takai, Yoshimi</creatorcontrib><description>E-cadherin is a key cell-cell adhesion molecule at adherens junctions (AJs) and undergoes endocytosis when AJs are disrupted by the action of extracellular signals. To elucidate the mechanism of this endocytosis, we developed here a new cell-free assay system for this reaction using the AJ-enriched fraction from rat liver. We found here that non-trans-interacting, but not trans-interacting, E-cadherin underwent endocytosis in a clathrin-dependent manner. The endocytosis of trans-interacting E-cadherin was inhibited by Rac and Cdc42 small G proteins, which were activated by trans-interacting E-cadherin or trans-interacting nectins, which are known to induce the formation of AJs in cooperation with E-cadherin. This inhibition was mediated by reorganization of the actin cytoskeleton by Rac and Cdc42 through IQGAP1, an actin filament-binding protein and a downstream target of Rac and Cdc42. These results indicate the important role of the Rac/Cdc42-IQGAP1 system in the dynamic organization and maintenance of the E-cadherin-based AJs.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.200401078</identifier><identifier>PMID: 15263019</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Actin Cytoskeleton ; Actins ; Adherens Junctions ; Animals ; Brain ; Cadherins ; Cadherins - metabolism ; Carrier Proteins - metabolism ; cdc42 GTP-Binding Protein - physiology ; Cell adhesion ; Cell membranes ; Cell-Free System ; Cells ; Clathrin-Coated Vesicles ; Cytosol ; Endocytosis ; GTP-Binding Proteins - physiology ; Guanine nucleotide dissociation inhibitors ; Liver ; Microfilaments ; Physiological regulation ; Proteins ; rac GTP-Binding Proteins - physiology ; ras GTPase-Activating Proteins ; Rats ; Signal transduction</subject><ispartof>The Journal of cell biology, 2004-07, Vol.166 (2), p.237-248</ispartof><rights>Copyright 2004 The Rockefeller University Press</rights><rights>Copyright The Rockerfeller University Press</rights><rights>Copyright Rockefeller University Press Jul 19, 2004</rights><rights>Copyright © 2004, The Rockefeller University Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c497t-2b73f122cd8c35bed235cf91891b9eedfbe8adfdab2232bdc0041728470dae893</citedby><cites>FETCH-LOGICAL-c497t-2b73f122cd8c35bed235cf91891b9eedfbe8adfdab2232bdc0041728470dae893</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15263019$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Izumi, Genkichi</creatorcontrib><creatorcontrib>Sakisaka, Toshiaki</creatorcontrib><creatorcontrib>Baba, Takeshi</creatorcontrib><creatorcontrib>Tanaka, Shintaro</creatorcontrib><creatorcontrib>Morimoto, Koji</creatorcontrib><creatorcontrib>Takai, Yoshimi</creatorcontrib><title>Endocytosis of E-Cadherin Regulated by Rac and Cdc42 Small G Proteins through IQGAP1 and Actin Filaments</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>E-cadherin is a key cell-cell adhesion molecule at adherens junctions (AJs) and undergoes endocytosis when AJs are disrupted by the action of extracellular signals. To elucidate the mechanism of this endocytosis, we developed here a new cell-free assay system for this reaction using the AJ-enriched fraction from rat liver. We found here that non-trans-interacting, but not trans-interacting, E-cadherin underwent endocytosis in a clathrin-dependent manner. The endocytosis of trans-interacting E-cadherin was inhibited by Rac and Cdc42 small G proteins, which were activated by trans-interacting E-cadherin or trans-interacting nectins, which are known to induce the formation of AJs in cooperation with E-cadherin. This inhibition was mediated by reorganization of the actin cytoskeleton by Rac and Cdc42 through IQGAP1, an actin filament-binding protein and a downstream target of Rac and Cdc42. These results indicate the important role of the Rac/Cdc42-IQGAP1 system in the dynamic organization and maintenance of the E-cadherin-based AJs.</description><subject>Actin Cytoskeleton</subject><subject>Actins</subject><subject>Adherens Junctions</subject><subject>Animals</subject><subject>Brain</subject><subject>Cadherins</subject><subject>Cadherins - metabolism</subject><subject>Carrier Proteins - metabolism</subject><subject>cdc42 GTP-Binding Protein - physiology</subject><subject>Cell adhesion</subject><subject>Cell membranes</subject><subject>Cell-Free System</subject><subject>Cells</subject><subject>Clathrin-Coated Vesicles</subject><subject>Cytosol</subject><subject>Endocytosis</subject><subject>GTP-Binding Proteins - physiology</subject><subject>Guanine nucleotide dissociation inhibitors</subject><subject>Liver</subject><subject>Microfilaments</subject><subject>Physiological regulation</subject><subject>Proteins</subject><subject>rac GTP-Binding Proteins - physiology</subject><subject>ras GTPase-Activating Proteins</subject><subject>Rats</subject><subject>Signal transduction</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkc1v0zAYhy0EYqVw5IaQtQO3DPu1kzgXpKrqyqRJjAFny19pUiXxsB2k_ve4tNqA03t4Hz3vxw-ht5RcUSLYx73RV0AIJ5TU4hla0JKTQlBOnqMFIUCLpoTyAr2KcU8yVnP2El3QEipGaLNA3Way3hySj33EvsWbYq1s50I_4Xu3mweVnMX6gO-VwWqyeG0NB_xtVMOAt_gu-OT6KeLUBT_vOnzzdbu6o3_IlUlZct0PanRTiq_Ri1YN0b051yX6cb35vv5c3H7Z3qxXt4XhTZ0K0DVrKYCxwrBSOwusNG1DRUN145xttRPKtlZpAAbamnwTrUHwmljlRMOW6NPJ-zDr0VmTZwc1yIfQjyocpFe9_Lcz9Z3c-V8Ssobljy7Rh7Mg-J-zi0mOfTRuGNTk_BxlVdVQ1vQ46fI_cO_nMOXjji4iuKh4hooTZIKPMbj2cRNK5DFAmQOUjwFm_v3f6z_R58Qy8O4E7GPy4alfAZBGsN-eTp-R</recordid><startdate>20040719</startdate><enddate>20040719</enddate><creator>Izumi, Genkichi</creator><creator>Sakisaka, Toshiaki</creator><creator>Baba, Takeshi</creator><creator>Tanaka, Shintaro</creator><creator>Morimoto, Koji</creator><creator>Takai, Yoshimi</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</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>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20040719</creationdate><title>Endocytosis of E-Cadherin Regulated by Rac and Cdc42 Small G Proteins through IQGAP1 and Actin Filaments</title><author>Izumi, Genkichi ; Sakisaka, Toshiaki ; Baba, Takeshi ; Tanaka, Shintaro ; Morimoto, Koji ; Takai, Yoshimi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c497t-2b73f122cd8c35bed235cf91891b9eedfbe8adfdab2232bdc0041728470dae893</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Actin Cytoskeleton</topic><topic>Actins</topic><topic>Adherens Junctions</topic><topic>Animals</topic><topic>Brain</topic><topic>Cadherins</topic><topic>Cadherins - metabolism</topic><topic>Carrier Proteins - metabolism</topic><topic>cdc42 GTP-Binding Protein - physiology</topic><topic>Cell adhesion</topic><topic>Cell membranes</topic><topic>Cell-Free System</topic><topic>Cells</topic><topic>Clathrin-Coated Vesicles</topic><topic>Cytosol</topic><topic>Endocytosis</topic><topic>GTP-Binding Proteins - physiology</topic><topic>Guanine nucleotide dissociation inhibitors</topic><topic>Liver</topic><topic>Microfilaments</topic><topic>Physiological regulation</topic><topic>Proteins</topic><topic>rac GTP-Binding Proteins - physiology</topic><topic>ras GTPase-Activating Proteins</topic><topic>Rats</topic><topic>Signal transduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Izumi, Genkichi</creatorcontrib><creatorcontrib>Sakisaka, Toshiaki</creatorcontrib><creatorcontrib>Baba, Takeshi</creatorcontrib><creatorcontrib>Tanaka, Shintaro</creatorcontrib><creatorcontrib>Morimoto, Koji</creatorcontrib><creatorcontrib>Takai, Yoshimi</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>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids 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>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>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Izumi, Genkichi</au><au>Sakisaka, Toshiaki</au><au>Baba, Takeshi</au><au>Tanaka, Shintaro</au><au>Morimoto, Koji</au><au>Takai, Yoshimi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Endocytosis of E-Cadherin Regulated by Rac and Cdc42 Small G Proteins through IQGAP1 and Actin Filaments</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>2004-07-19</date><risdate>2004</risdate><volume>166</volume><issue>2</issue><spage>237</spage><epage>248</epage><pages>237-248</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>E-cadherin is a key cell-cell adhesion molecule at adherens junctions (AJs) and undergoes endocytosis when AJs are disrupted by the action of extracellular signals. To elucidate the mechanism of this endocytosis, we developed here a new cell-free assay system for this reaction using the AJ-enriched fraction from rat liver. We found here that non-trans-interacting, but not trans-interacting, E-cadherin underwent endocytosis in a clathrin-dependent manner. The endocytosis of trans-interacting E-cadherin was inhibited by Rac and Cdc42 small G proteins, which were activated by trans-interacting E-cadherin or trans-interacting nectins, which are known to induce the formation of AJs in cooperation with E-cadherin. This inhibition was mediated by reorganization of the actin cytoskeleton by Rac and Cdc42 through IQGAP1, an actin filament-binding protein and a downstream target of Rac and Cdc42. These results indicate the important role of the Rac/Cdc42-IQGAP1 system in the dynamic organization and maintenance of the E-cadherin-based AJs.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>15263019</pmid><doi>10.1083/jcb.200401078</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9525 |
| ispartof | The Journal of cell biology, 2004-07, Vol.166 (2), p.237-248 |
| issn | 0021-9525 1540-8140 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2172308 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Actin Cytoskeleton Actins Adherens Junctions Animals Brain Cadherins Cadherins - metabolism Carrier Proteins - metabolism cdc42 GTP-Binding Protein - physiology Cell adhesion Cell membranes Cell-Free System Cells Clathrin-Coated Vesicles Cytosol Endocytosis GTP-Binding Proteins - physiology Guanine nucleotide dissociation inhibitors Liver Microfilaments Physiological regulation Proteins rac GTP-Binding Proteins - physiology ras GTPase-Activating Proteins Rats Signal transduction |
| title | Endocytosis of E-Cadherin Regulated by Rac and Cdc42 Small G Proteins through IQGAP1 and Actin Filaments |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-29T04%3A06%3A38IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Endocytosis%20of%20E-Cadherin%20Regulated%20by%20Rac%20and%20Cdc42%20Small%20G%20Proteins%20through%20IQGAP1%20and%20Actin%20Filaments&rft.jtitle=The%20Journal%20of%20cell%20biology&rft.au=Izumi,%20Genkichi&rft.date=2004-07-19&rft.volume=166&rft.issue=2&rft.spage=237&rft.epage=248&rft.pages=237-248&rft.issn=0021-9525&rft.eissn=1540-8140&rft.coden=JCLBA3&rft_id=info:doi/10.1083/jcb.200401078&rft_dat=%3Cjstor_pubme%3E1622098%3C/jstor_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=217084864&rft_id=info:pmid/15263019&rft_jstor_id=1622098&rfr_iscdi=true |