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XRab40 and XCullin5 form a ubiquitin ligase complex essential for the noncanonical Wnt pathway
Rab GTPases are key regulators of intracellular membrane trafficking. We sought to elucidate the roles of Rab GTPases in Xenopus gastrulation, and found that a Xenopus homolog of Rab40 (XRab40) is required for normal gastrulation. XRab40 is localized at the Golgi apparatus and interacts with Elongin...
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Published in: | The EMBO journal 2007-08, Vol.26 (15), p.3592-3606 |
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container_title | The EMBO journal |
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creator | Lee, Rebecca Hui Kwan Iioka, Hidekazu Ohashi, Masato Iemura, Shun-ichiro Natsume, Tohru Kinoshita, Noriyuki |
description | Rab GTPases are key regulators of intracellular membrane trafficking. We sought to elucidate the roles of Rab GTPases in
Xenopus
gastrulation, and found that a
Xenopus
homolog of Rab40 (XRab40) is required for normal gastrulation. XRab40 is localized at the Golgi apparatus and interacts with ElonginB/C and Cullin5 to form a ubiquitin ligase. XRab40/XCullin5 functions cooperatively and regulates the ubiquitination and localization of Rap2 GTPase. Furthermore, XRab40/XCullin5 regulates the membrane localization of Dishevelled (Dsh), a key signaling molecule in the Wnt pathway, through Rap2 and its effector Misshapen/Nck‐interacting kinase (XMINK). XMINK interacts with Dsh, and is translocated to the plasma membrane by Wnt activation. We propose a novel signaling cascade consisting of XRab40/XCullin5, Rap2 and XMINK, which plays a crucial role in the regulation of the noncanonical Wnt pathway. |
doi_str_mv | 10.1038/sj.emboj.7601781 |
format | article |
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Xenopus
gastrulation, and found that a
Xenopus
homolog of Rab40 (XRab40) is required for normal gastrulation. XRab40 is localized at the Golgi apparatus and interacts with ElonginB/C and Cullin5 to form a ubiquitin ligase. XRab40/XCullin5 functions cooperatively and regulates the ubiquitination and localization of Rap2 GTPase. Furthermore, XRab40/XCullin5 regulates the membrane localization of Dishevelled (Dsh), a key signaling molecule in the Wnt pathway, through Rap2 and its effector Misshapen/Nck‐interacting kinase (XMINK). XMINK interacts with Dsh, and is translocated to the plasma membrane by Wnt activation. We propose a novel signaling cascade consisting of XRab40/XCullin5, Rap2 and XMINK, which plays a crucial role in the regulation of the noncanonical Wnt pathway.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1038/sj.emboj.7601781</identifier><identifier>PMID: 17627283</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Cellular biology ; EMBO11 ; EMBO37 ; gastrulation ; Membrane Proteins - chemistry ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Membranes ; Molecular biology ; Molecular Sequence Data ; Protein Binding ; Rab GTPase ; RNA, Messenger - genetics ; Sequence Homology, Amino Acid ; Signal transduction ; Substrate Specificity ; Two-Hybrid System Techniques ; Ubiquitin - metabolism ; Ubiquitin-Protein Ligases - metabolism ; ubiquitination ; Wnt Proteins - metabolism ; Wnt signaling ; Xenopus</subject><ispartof>The EMBO journal, 2007-08, Vol.26 (15), p.3592-3606</ispartof><rights>European Molecular Biology Organization 2007</rights><rights>Copyright © 2007 European Molecular Biology Organization</rights><rights>Copyright Nature Publishing Group Aug 8, 2007</rights><rights>Copyright © 2007, European Molecular Biology Organization 2007</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6701-d3d06b6adcbf2245b5e5019a8b2cef8f4fd6bda2f2ba6b9b271a38a0675b291b3</citedby><cites>FETCH-LOGICAL-c6701-d3d06b6adcbf2245b5e5019a8b2cef8f4fd6bda2f2ba6b9b271a38a0675b291b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1949004/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1949004/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17627283$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lee, Rebecca Hui Kwan</creatorcontrib><creatorcontrib>Iioka, Hidekazu</creatorcontrib><creatorcontrib>Ohashi, Masato</creatorcontrib><creatorcontrib>Iemura, Shun-ichiro</creatorcontrib><creatorcontrib>Natsume, Tohru</creatorcontrib><creatorcontrib>Kinoshita, Noriyuki</creatorcontrib><title>XRab40 and XCullin5 form a ubiquitin ligase complex essential for the noncanonical Wnt pathway</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>Rab GTPases are key regulators of intracellular membrane trafficking. We sought to elucidate the roles of Rab GTPases in
Xenopus
gastrulation, and found that a
Xenopus
homolog of Rab40 (XRab40) is required for normal gastrulation. XRab40 is localized at the Golgi apparatus and interacts with ElonginB/C and Cullin5 to form a ubiquitin ligase. XRab40/XCullin5 functions cooperatively and regulates the ubiquitination and localization of Rap2 GTPase. Furthermore, XRab40/XCullin5 regulates the membrane localization of Dishevelled (Dsh), a key signaling molecule in the Wnt pathway, through Rap2 and its effector Misshapen/Nck‐interacting kinase (XMINK). XMINK interacts with Dsh, and is translocated to the plasma membrane by Wnt activation. We propose a novel signaling cascade consisting of XRab40/XCullin5, Rap2 and XMINK, which plays a crucial role in the regulation of the noncanonical Wnt pathway.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Cellular biology</subject><subject>EMBO11</subject><subject>EMBO37</subject><subject>gastrulation</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Membranes</subject><subject>Molecular biology</subject><subject>Molecular Sequence Data</subject><subject>Protein Binding</subject><subject>Rab GTPase</subject><subject>RNA, Messenger - genetics</subject><subject>Sequence Homology, Amino Acid</subject><subject>Signal transduction</subject><subject>Substrate Specificity</subject><subject>Two-Hybrid System Techniques</subject><subject>Ubiquitin - metabolism</subject><subject>Ubiquitin-Protein Ligases - metabolism</subject><subject>ubiquitination</subject><subject>Wnt Proteins - metabolism</subject><subject>Wnt signaling</subject><subject>Xenopus</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><recordid>eNqFkUtv1DAUhSMEokNhzwZksWCXwXbiRzZIMCqFUorEQ-0K6zpxZhwSZ2ontPPvcclopiChbmzJ5zvHx75J8pTgOcGZfBWauel038wFx0RIci-ZkZzjlGLB7iczTDlJcyKLg-RRCA3GmElBHiYHRHAqqMxmyY-LL6BzjMBV6GIxtq11DNW97xCgUdvL0Q7WodYuIRhU9t26NdfIhGDcYKG9IdGwMsj1roS42DIenrsBrWFYXcHmcfKghjaYJ9v9MPn-7ujb4n16-vn4w-LNaVpygUlaZRXmmkNV6prSnGlmGCYFSE1LU8s6ryuuK6A11cB1oakgkEnAXDBNC6Kzw-T1lLsedWeqMtbz0Kq1tx34jerBqr8VZ1dq2f9SpMgLjPMY8HIb4PvL0YRBdTaUpm3BmX4MikvCMBb0TpAUIpdZnkXwxT9g04_exV-IDKMsvptECE9Q6fsQvKl3lQlWNyNWoVF_Rqy2I46W57efujdsZxqBYgKubGs2dwaqo09vT_bhZPKGaHNL42-V_n-hZ5PHwTB6s7twr6eTbsNgrncy-J-Ki0wwdX52rE44k1_P-EfFst_FeeBM</recordid><startdate>20070808</startdate><enddate>20070808</enddate><creator>Lee, Rebecca Hui Kwan</creator><creator>Iioka, Hidekazu</creator><creator>Ohashi, Masato</creator><creator>Iemura, Shun-ichiro</creator><creator>Natsume, Tohru</creator><creator>Kinoshita, Noriyuki</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>Nature Publishing Group</general><scope>BSCLL</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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20070808</creationdate><title>XRab40 and XCullin5 form a ubiquitin ligase complex essential for the noncanonical Wnt pathway</title><author>Lee, Rebecca Hui Kwan ; Iioka, Hidekazu ; Ohashi, Masato ; Iemura, Shun-ichiro ; Natsume, Tohru ; Kinoshita, Noriyuki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6701-d3d06b6adcbf2245b5e5019a8b2cef8f4fd6bda2f2ba6b9b271a38a0675b291b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Cellular biology</topic><topic>EMBO11</topic><topic>EMBO37</topic><topic>gastrulation</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Membranes</topic><topic>Molecular biology</topic><topic>Molecular Sequence Data</topic><topic>Protein Binding</topic><topic>Rab GTPase</topic><topic>RNA, Messenger - genetics</topic><topic>Sequence Homology, Amino Acid</topic><topic>Signal transduction</topic><topic>Substrate Specificity</topic><topic>Two-Hybrid System Techniques</topic><topic>Ubiquitin - metabolism</topic><topic>Ubiquitin-Protein Ligases - metabolism</topic><topic>ubiquitination</topic><topic>Wnt Proteins - metabolism</topic><topic>Wnt signaling</topic><topic>Xenopus</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lee, Rebecca Hui Kwan</creatorcontrib><creatorcontrib>Iioka, Hidekazu</creatorcontrib><creatorcontrib>Ohashi, Masato</creatorcontrib><creatorcontrib>Iemura, Shun-ichiro</creatorcontrib><creatorcontrib>Natsume, Tohru</creatorcontrib><creatorcontrib>Kinoshita, Noriyuki</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>ProQuest Health and Medical</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>ProQuest research library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>ProQuest Biological Science Journals</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lee, Rebecca Hui Kwan</au><au>Iioka, Hidekazu</au><au>Ohashi, Masato</au><au>Iemura, Shun-ichiro</au><au>Natsume, Tohru</au><au>Kinoshita, Noriyuki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>XRab40 and XCullin5 form a ubiquitin ligase complex essential for the noncanonical Wnt pathway</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2007-08-08</date><risdate>2007</risdate><volume>26</volume><issue>15</issue><spage>3592</spage><epage>3606</epage><pages>3592-3606</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>Rab GTPases are key regulators of intracellular membrane trafficking. We sought to elucidate the roles of Rab GTPases in
Xenopus
gastrulation, and found that a
Xenopus
homolog of Rab40 (XRab40) is required for normal gastrulation. XRab40 is localized at the Golgi apparatus and interacts with ElonginB/C and Cullin5 to form a ubiquitin ligase. XRab40/XCullin5 functions cooperatively and regulates the ubiquitination and localization of Rap2 GTPase. Furthermore, XRab40/XCullin5 regulates the membrane localization of Dishevelled (Dsh), a key signaling molecule in the Wnt pathway, through Rap2 and its effector Misshapen/Nck‐interacting kinase (XMINK). XMINK interacts with Dsh, and is translocated to the plasma membrane by Wnt activation. We propose a novel signaling cascade consisting of XRab40/XCullin5, Rap2 and XMINK, which plays a crucial role in the regulation of the noncanonical Wnt pathway.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>17627283</pmid><doi>10.1038/sj.emboj.7601781</doi><tpages>15</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Animals Cellular biology EMBO11 EMBO37 gastrulation Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Membranes Molecular biology Molecular Sequence Data Protein Binding Rab GTPase RNA, Messenger - genetics Sequence Homology, Amino Acid Signal transduction Substrate Specificity Two-Hybrid System Techniques Ubiquitin - metabolism Ubiquitin-Protein Ligases - metabolism ubiquitination Wnt Proteins - metabolism Wnt signaling Xenopus |
title | XRab40 and XCullin5 form a ubiquitin ligase complex essential for the noncanonical Wnt pathway |
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