Cloning, expression, and localization of a novel γ-adaptin-like molecule
We describe the cloning, expression, and localization of γ 2-adaptin, a novel isoform of γ-adaptin. The predicted human and mouse γ 2-adaptin proteins are ∼90 kDa and 64.4% and 61.7% identical to γ-adaptin, respectively. γ 2-Adaptin was localized to the Golgi, its localization distinct from γ-adapti...
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| Veröffentlicht in: | FEBS letters 1998-09, Vol.435 (2), p.263-268 |
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| container_title | FEBS letters |
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| creator | Lewin, David A. Sheff, David Ooi, Chean Eng Whitney, J.Andrew Yamamoto, Ellen Chicione, Linda M. Webster, Paul Bonifacino, Juan S. Mellman, Ira |
| description | We describe the cloning, expression, and localization of γ
2-adaptin, a novel isoform of γ-adaptin. The predicted human and mouse γ
2-adaptin proteins are ∼90 kDa and 64.4% and 61.7% identical to γ-adaptin, respectively. γ
2-Adaptin was localized to the Golgi, its localization distinct from γ-adaptin. The membrane association of γ- and γ
2-adaptin could further be distinguished by differential sensitivity to the fungal metabolite brefeldin A, γ
2-adaptin binding being insensitive to drug treatment. Together, these results suggest that γ
2-adaptin plays a role in membrane transport distinct from that played by γ-adaptin. |
| doi_str_mv | 10.1016/S0014-5793(98)01083-7 |
| format | Article |
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2-adaptin, a novel isoform of γ-adaptin. The predicted human and mouse γ
2-adaptin proteins are ∼90 kDa and 64.4% and 61.7% identical to γ-adaptin, respectively. γ
2-Adaptin was localized to the Golgi, its localization distinct from γ-adaptin. The membrane association of γ- and γ
2-adaptin could further be distinguished by differential sensitivity to the fungal metabolite brefeldin A, γ
2-adaptin binding being insensitive to drug treatment. Together, these results suggest that γ
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2-adaptin, a novel isoform of γ-adaptin. The predicted human and mouse γ
2-adaptin proteins are ∼90 kDa and 64.4% and 61.7% identical to γ-adaptin, respectively. γ
2-Adaptin was localized to the Golgi, its localization distinct from γ-adaptin. The membrane association of γ- and γ
2-adaptin could further be distinguished by differential sensitivity to the fungal metabolite brefeldin A, γ
2-adaptin binding being insensitive to drug treatment. Together, these results suggest that γ
2-adaptin plays a role in membrane transport distinct from that played by γ-adaptin.</description><subject>Adaptin</subject><subject>Adaptor</subject><subject>Adaptor Protein Complex gamma Subunits</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Cloning, Molecular</subject><subject>Gene Expression</subject><subject>Golgi</subject><subject>HeLa Cells</subject><subject>Human</subject><subject>Humans</subject><subject>Immunohistochemistry</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Mouse</subject><subject>Organ Specificity</subject><subject>Sequence Analysis</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE1OwzAQhS0EglI4AlJWCKQG_JPE9gpBxZ-ExAJYW649RgY3LnFbKNfiHpyJpK3Ywmo08968GX0IHRB8QjCpTh8wJkVecsmOpDjGBAuW8w3UI4KznBWV2ES9X8sO2k3pBbe9IHIbbUteUUlpD90OQ6x9_TzI4GPSQEo-1oNM1zYL0ejgP_W0nWTRZTqr4xxC9v2Va6snU1_nwb9CNo4BzCzAHtpyOiTYX9c-erq6fBze5Hf317fD87vcFJzznHHMK-kslYI7B6VzoixGAqgkVhPLNQhcmQJbLUhpjZEOjGOUGj2iVAjJ-uhwlTtp4tsM0lSNfTIQgq4hzpLiTLJSirI1liujaWJKDTg1afxYNwtFsOoQqiVC1fFRUqglwna9jw7WB2ajMdjfrTWzVr9Z6e8-wOJ_oerq8oIulU6QYjnuTp2toqAFNvfQqGQ81Aasb8BMlY3-j2d_AMsMlVQ</recordid><startdate>19980918</startdate><enddate>19980918</enddate><creator>Lewin, David A.</creator><creator>Sheff, David</creator><creator>Ooi, Chean Eng</creator><creator>Whitney, J.Andrew</creator><creator>Yamamoto, Ellen</creator><creator>Chicione, Linda M.</creator><creator>Webster, Paul</creator><creator>Bonifacino, Juan S.</creator><creator>Mellman, Ira</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>19980918</creationdate><title>Cloning, expression, and localization of a novel γ-adaptin-like molecule</title><author>Lewin, David A. ; Sheff, David ; Ooi, Chean Eng ; Whitney, J.Andrew ; Yamamoto, Ellen ; Chicione, Linda M. ; Webster, Paul ; Bonifacino, Juan S. ; Mellman, Ira</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4777-370769fd2987ffe5ff854b8e291da1d7ae806c40da815dcc9fecf322cab228893</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Adaptin</topic><topic>Adaptor</topic><topic>Adaptor Protein Complex gamma Subunits</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Cloning, Molecular</topic><topic>Gene Expression</topic><topic>Golgi</topic><topic>HeLa Cells</topic><topic>Human</topic><topic>Humans</topic><topic>Immunohistochemistry</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Mouse</topic><topic>Organ Specificity</topic><topic>Sequence Analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lewin, David A.</creatorcontrib><creatorcontrib>Sheff, David</creatorcontrib><creatorcontrib>Ooi, Chean Eng</creatorcontrib><creatorcontrib>Whitney, J.Andrew</creatorcontrib><creatorcontrib>Yamamoto, Ellen</creatorcontrib><creatorcontrib>Chicione, Linda M.</creatorcontrib><creatorcontrib>Webster, Paul</creatorcontrib><creatorcontrib>Bonifacino, Juan S.</creatorcontrib><creatorcontrib>Mellman, Ira</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lewin, David A.</au><au>Sheff, David</au><au>Ooi, Chean Eng</au><au>Whitney, J.Andrew</au><au>Yamamoto, Ellen</au><au>Chicione, Linda M.</au><au>Webster, Paul</au><au>Bonifacino, Juan S.</au><au>Mellman, Ira</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning, expression, and localization of a novel γ-adaptin-like molecule</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1998-09-18</date><risdate>1998</risdate><volume>435</volume><issue>2</issue><spage>263</spage><epage>268</epage><pages>263-268</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>We describe the cloning, expression, and localization of γ
2-adaptin, a novel isoform of γ-adaptin. The predicted human and mouse γ
2-adaptin proteins are ∼90 kDa and 64.4% and 61.7% identical to γ-adaptin, respectively. γ
2-Adaptin was localized to the Golgi, its localization distinct from γ-adaptin. The membrane association of γ- and γ
2-adaptin could further be distinguished by differential sensitivity to the fungal metabolite brefeldin A, γ
2-adaptin binding being insensitive to drug treatment. Together, these results suggest that γ
2-adaptin plays a role in membrane transport distinct from that played by γ-adaptin.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>9762922</pmid><doi>10.1016/S0014-5793(98)01083-7</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Wiley Journals; Elsevier ScienceDirect Journals Complete; Wiley Online Library Free Content; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Adaptin Adaptor Adaptor Protein Complex gamma Subunits Amino Acid Sequence Animals Cloning, Molecular Gene Expression Golgi HeLa Cells Human Humans Immunohistochemistry Membrane Proteins - genetics Membrane Proteins - metabolism Mice Molecular Sequence Data Mouse Organ Specificity Sequence Analysis |
| title | Cloning, expression, and localization of a novel γ-adaptin-like molecule |
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