Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation
Internalization of diverse transmembrane cargos from the plasma membrane requires a similarly diverse array of specialized adaptors, yet only a few adaptors have been characterized. We report the identification of the muniscin family of endocytic adaptors that is conserved from yeast to human beings...
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| Veröffentlicht in: | The EMBO journal 2009-10, Vol.28 (20), p.3103-3116 |
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| creator | Reider, Amanda Barker, Sarah L Mishra, Sanjay K Im, Young Jun Maldonado-Báez, Lymarie Hurley, James H Traub, Linton M Wendland, Beverly |
| description | Internalization of diverse transmembrane cargos from the plasma membrane requires a similarly diverse array of specialized adaptors, yet only a few adaptors have been characterized. We report the identification of the muniscin family of endocytic adaptors that is conserved from yeast to human beings. Solving the structures of yeast muniscin domains confirmed the unique combination of an N‐terminal domain homologous to the crescent‐shaped membrane‐tubulating EFC/F‐BAR domains and a C‐terminal domain homologous to cargo‐binding μ homology domains (μHDs).
In vitro
and
in vivo
assays confirmed membrane‐tubulation activity for muniscin EFC/F‐BAR domains. The μHD domain has conserved interactions with the endocytic adaptor/scaffold Ede1/eps15, which influences muniscin localization. The transmembrane protein Mid2, earlier implicated in polarized Rho1 signalling, was identified as a cargo of the yeast adaptor protein. These and other data suggest a model in which the muniscins provide a combined adaptor/membrane‐tubulation activity that is important for regulating endocytosis. |
| doi_str_mv | 10.1038/emboj.2009.248 |
| format | Article |
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In vitro
and
in vivo
assays confirmed membrane‐tubulation activity for muniscin EFC/F‐BAR domains. The μHD domain has conserved interactions with the endocytic adaptor/scaffold Ede1/eps15, which influences muniscin localization. The transmembrane protein Mid2, earlier implicated in polarized Rho1 signalling, was identified as a cargo of the yeast adaptor protein. These and other data suggest a model in which the muniscins provide a combined adaptor/membrane‐tubulation activity that is important for regulating endocytosis.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1038/emboj.2009.248</identifier><identifier>PMID: 19713939</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>adaptor ; BASIC BIOLOGICAL SCIENCES ; Binding sites ; CARGO ; EMBO20 ; EMBO40 ; endocytosis ; Endocytosis - physiology ; F-BAR ; GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE ; HeLa Cells ; Humans ; IN VITRO ; IN VIVO ; Membrane Proteins ; MEMBRANES ; Molecular biology ; PLASMA ; Protein Binding ; Protein Structure, Secondary ; PROTEINS ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Signal transduction ; Syp1 ; Two-Hybrid System Techniques ; YEASTS ; μHD</subject><ispartof>The EMBO journal, 2009-10, Vol.28 (20), p.3103-3116</ispartof><rights>European Molecular Biology Organization 2009</rights><rights>Copyright © 2009 European Molecular Biology Organization</rights><rights>Copyright Nature Publishing Group Oct 21, 2009</rights><rights>Copyright © 2009, European Molecular Biology Organization 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5958-ad71c74bc0e6f2e0bf75cc3700b3397badee83103e80e9ef45c5cc94af21ccf43</citedby><cites>FETCH-LOGICAL-c5958-ad71c74bc0e6f2e0bf75cc3700b3397badee83103e80e9ef45c5cc94af21ccf43</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/PMC2771086/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2771086/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,41120,42189,45574,45575,46409,46833,51576,53791,53793</link.rule.ids><linktorsrc>$$Uhttps://doi.org/10.1038/emboj.2009.248$$EView_record_in_Springer_Nature$$FView_record_in_$$GSpringer_Nature</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19713939$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/1006195$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Reider, Amanda</creatorcontrib><creatorcontrib>Barker, Sarah L</creatorcontrib><creatorcontrib>Mishra, Sanjay K</creatorcontrib><creatorcontrib>Im, Young Jun</creatorcontrib><creatorcontrib>Maldonado-Báez, Lymarie</creatorcontrib><creatorcontrib>Hurley, James H</creatorcontrib><creatorcontrib>Traub, Linton M</creatorcontrib><creatorcontrib>Wendland, Beverly</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States)</creatorcontrib><title>Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>Internalization of diverse transmembrane cargos from the plasma membrane requires a similarly diverse array of specialized adaptors, yet only a few adaptors have been characterized. We report the identification of the muniscin family of endocytic adaptors that is conserved from yeast to human beings. Solving the structures of yeast muniscin domains confirmed the unique combination of an N‐terminal domain homologous to the crescent‐shaped membrane‐tubulating EFC/F‐BAR domains and a C‐terminal domain homologous to cargo‐binding μ homology domains (μHDs).
In vitro
and
in vivo
assays confirmed membrane‐tubulation activity for muniscin EFC/F‐BAR domains. The μHD domain has conserved interactions with the endocytic adaptor/scaffold Ede1/eps15, which influences muniscin localization. The transmembrane protein Mid2, earlier implicated in polarized Rho1 signalling, was identified as a cargo of the yeast adaptor protein. These and other data suggest a model in which the muniscins provide a combined adaptor/membrane‐tubulation activity that is important for regulating endocytosis.</description><subject>adaptor</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>Binding sites</subject><subject>CARGO</subject><subject>EMBO20</subject><subject>EMBO40</subject><subject>endocytosis</subject><subject>Endocytosis - physiology</subject><subject>F-BAR</subject><subject>GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>IN VITRO</subject><subject>IN VIVO</subject><subject>Membrane Proteins</subject><subject>MEMBRANES</subject><subject>Molecular biology</subject><subject>PLASMA</subject><subject>Protein Binding</subject><subject>Protein Structure, Secondary</subject><subject>PROTEINS</subject><subject>Saccharomyces cerevisiae Proteins - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Signal transduction</subject><subject>Syp1</subject><subject>Two-Hybrid System Techniques</subject><subject>YEASTS</subject><subject>μHD</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkc2P0zAQxS0EYsvClSOyOHBL186X4wsSWy3Lxy4IAULiYjnOpHVJ7GI7hf73OE3VLgfEybL9mzdv5iH0lJI5JVl1AX1t1_OUED5P8-oemtG8JElKWHEfzUha0iSnFT9Dj7xfE0KKitGH6IxyRjOe8Rmyn3cbirXHEitrPLgtNBhMY9UuaIVlIzfBOhxWMoxAkNp43Nh-f2qztd1YoA1W0i0t9tCBCtoaLE2D--jOSQM4DPXQyfH9MXrQys7Dk8N5jr6-vvqyeJPcfLx-u3h1k6iCF1UiG0YVy2tFoGxTIHXLCqUyRkidZZzVsgGosrgBqAhwaPNCxX-eyzalSrV5do5eTrqboe6hUWCCk53YON1LtxNWavH3j9ErsbRbkTJGSVVGgeeTgPVBC690ALWKGzBxPkEJKSkvIvTi0MXZnwP4IHrtFXRdHNoOXpSs5CXn_KR2BNd2cCZuQESdtCQ5HT3PJ0g5672D9miXEjGmLfZpizFtEdOOBc_uDnnCD_FGgE3AL93B7j9y4ur28t14maQvpkofi8wS3B3D_zJzGNHIMDg4NttjJ9lkgrQP8PvISPcj7ipjhfj24VqQ97efKkq-i0X2BzS-5NY</recordid><startdate>20091021</startdate><enddate>20091021</enddate><creator>Reider, Amanda</creator><creator>Barker, Sarah L</creator><creator>Mishra, Sanjay K</creator><creator>Im, Young Jun</creator><creator>Maldonado-Báez, Lymarie</creator><creator>Hurley, James H</creator><creator>Traub, Linton M</creator><creator>Wendland, Beverly</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>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>20091021</creationdate><title>Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation</title><author>Reider, Amanda ; 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(ANL), Argonne, IL (United States)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2009-10-21</date><risdate>2009</risdate><volume>28</volume><issue>20</issue><spage>3103</spage><epage>3116</epage><pages>3103-3116</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>Internalization of diverse transmembrane cargos from the plasma membrane requires a similarly diverse array of specialized adaptors, yet only a few adaptors have been characterized. We report the identification of the muniscin family of endocytic adaptors that is conserved from yeast to human beings. Solving the structures of yeast muniscin domains confirmed the unique combination of an N‐terminal domain homologous to the crescent‐shaped membrane‐tubulating EFC/F‐BAR domains and a C‐terminal domain homologous to cargo‐binding μ homology domains (μHDs).
In vitro
and
in vivo
assays confirmed membrane‐tubulation activity for muniscin EFC/F‐BAR domains. The μHD domain has conserved interactions with the endocytic adaptor/scaffold Ede1/eps15, which influences muniscin localization. The transmembrane protein Mid2, earlier implicated in polarized Rho1 signalling, was identified as a cargo of the yeast adaptor protein. These and other data suggest a model in which the muniscins provide a combined adaptor/membrane‐tubulation activity that is important for regulating endocytosis.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>19713939</pmid><doi>10.1038/emboj.2009.248</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| source | Springer Nature OA Free Journals |
| subjects | adaptor BASIC BIOLOGICAL SCIENCES Binding sites CARGO EMBO20 EMBO40 endocytosis Endocytosis - physiology F-BAR GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE HeLa Cells Humans IN VITRO IN VIVO Membrane Proteins MEMBRANES Molecular biology PLASMA Protein Binding Protein Structure, Secondary PROTEINS Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Signal transduction Syp1 Two-Hybrid System Techniques YEASTS μHD |
| title | Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation |
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