Role of NH2-terminal hydrophobic motif in the subcellular localization of ATP-binding cassette protein subfamily D: common features in eukaryotic organisms
In mammals, four ATP-binding cassette (ABC) proteins belonging to subfamily D have been identified. ABCD1-3 possesses the NH2-terminal hydrophobic region and are targeted to peroxisomes, while ABCD4 lacking the region is targeted to the endoplasmic reticulum (ER). Based on hydropathy plot analysis,...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2014-10, Vol.453 (3), p.612-618 |
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| creator | Lee, Asaka Asahina, Kota Okamoto, Takumi Kawaguchi, Kosuke Kostsin, Dzmitry G Kashiwayama, Yoshinori Takanashi, Kojiro Yazaki, Kazufumi Imanaka, Tsuneo Morita, Masashi |
| description | In mammals, four ATP-binding cassette (ABC) proteins belonging to subfamily D have been identified. ABCD1-3 possesses the NH2-terminal hydrophobic region and are targeted to peroxisomes, while ABCD4 lacking the region is targeted to the endoplasmic reticulum (ER). Based on hydropathy plot analysis, we found that several eukaryotes have ABCD protein homologs lacking the NH2-terminal hydrophobic segment (H0 motif). To investigate whether the role of the NH2-terminal H0 motif in subcellular localization is conserved across species, we expressed ABCD proteins from several species (metazoan, plant and fungi) in fusion with GFP in CHO cells and examined their subcellular localization. ABCD proteins possessing the NH2-terminal H0 motif were localized to peroxisomes, while ABCD proteins lacking this region lost this capacity. In addition, the deletion of the NH2-terminal H0 motif of ABCD protein resulted in their localization to the ER. These results suggest that the role of the NH2-terminal H0 motif in organelle targeting is widely conserved in living organisms. |
| doi_str_mv | 10.1016/j.bbrc.2014.09.133 |
| format | Article |
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ABCD1-3 possesses the NH2-terminal hydrophobic region and are targeted to peroxisomes, while ABCD4 lacking the region is targeted to the endoplasmic reticulum (ER). Based on hydropathy plot analysis, we found that several eukaryotes have ABCD protein homologs lacking the NH2-terminal hydrophobic segment (H0 motif). To investigate whether the role of the NH2-terminal H0 motif in subcellular localization is conserved across species, we expressed ABCD proteins from several species (metazoan, plant and fungi) in fusion with GFP in CHO cells and examined their subcellular localization. ABCD proteins possessing the NH2-terminal H0 motif were localized to peroxisomes, while ABCD proteins lacking this region lost this capacity. In addition, the deletion of the NH2-terminal H0 motif of ABCD protein resulted in their localization to the ER. These results suggest that the role of the NH2-terminal H0 motif in organelle targeting is widely conserved in living organisms.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2014.09.133</identifier><identifier>PMID: 25301552</identifier><language>eng</language><publisher>United States</publisher><subject>Animals ; Arabidopsis - metabolism ; ATP-Binding Cassette Transporters - chemistry ; ATP-Binding Cassette Transporters - metabolism ; Caenorhabditis elegans - metabolism ; CHO Cells ; Cricetinae ; Cricetulus ; Eukaryotic Cells - metabolism ; Fluorescent Antibody Technique ; Hydrophobic and Hydrophilic Interactions ; Subcellular Fractions - metabolism</subject><ispartof>Biochemical and biophysical research communications, 2014-10, Vol.453 (3), p.612-618</ispartof><rights>Copyright © 2014 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c439t-38fdd9a05f8b24003a25fa2cfe530b09f62d8e4a420810fb741c019abb41b7583</citedby><cites>FETCH-LOGICAL-c439t-38fdd9a05f8b24003a25fa2cfe530b09f62d8e4a420810fb741c019abb41b7583</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25301552$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lee, Asaka</creatorcontrib><creatorcontrib>Asahina, Kota</creatorcontrib><creatorcontrib>Okamoto, Takumi</creatorcontrib><creatorcontrib>Kawaguchi, Kosuke</creatorcontrib><creatorcontrib>Kostsin, Dzmitry G</creatorcontrib><creatorcontrib>Kashiwayama, Yoshinori</creatorcontrib><creatorcontrib>Takanashi, Kojiro</creatorcontrib><creatorcontrib>Yazaki, Kazufumi</creatorcontrib><creatorcontrib>Imanaka, Tsuneo</creatorcontrib><creatorcontrib>Morita, Masashi</creatorcontrib><title>Role of NH2-terminal hydrophobic motif in the subcellular localization of ATP-binding cassette protein subfamily D: common features in eukaryotic organisms</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>In mammals, four ATP-binding cassette (ABC) proteins belonging to subfamily D have been identified. ABCD1-3 possesses the NH2-terminal hydrophobic region and are targeted to peroxisomes, while ABCD4 lacking the region is targeted to the endoplasmic reticulum (ER). Based on hydropathy plot analysis, we found that several eukaryotes have ABCD protein homologs lacking the NH2-terminal hydrophobic segment (H0 motif). To investigate whether the role of the NH2-terminal H0 motif in subcellular localization is conserved across species, we expressed ABCD proteins from several species (metazoan, plant and fungi) in fusion with GFP in CHO cells and examined their subcellular localization. ABCD proteins possessing the NH2-terminal H0 motif were localized to peroxisomes, while ABCD proteins lacking this region lost this capacity. In addition, the deletion of the NH2-terminal H0 motif of ABCD protein resulted in their localization to the ER. These results suggest that the role of the NH2-terminal H0 motif in organelle targeting is widely conserved in living organisms.</description><subject>Animals</subject><subject>Arabidopsis - metabolism</subject><subject>ATP-Binding Cassette Transporters - chemistry</subject><subject>ATP-Binding Cassette Transporters - metabolism</subject><subject>Caenorhabditis elegans - metabolism</subject><subject>CHO Cells</subject><subject>Cricetinae</subject><subject>Cricetulus</subject><subject>Eukaryotic Cells - metabolism</subject><subject>Fluorescent Antibody Technique</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Subcellular Fractions - metabolism</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kc1u1DAURi0EotPCC7BAXrJJuP5JJmZXFdoiVRShIrGzbMfueHDiwXYW01fhZeuohdXdfOe79-og9I5AS4D0H_et1sm0FAhvQbSEsRdoQ0BAQwnwl2gDAH1DBfl1gk5z3gMQwnvxGp3QjgHpOrpBf3_EYHF0-Ns1bYpNk59VwLvjmOJhF7U3eIrFO-xnXHYW50UbG8ISVMIhGhX8gyo-zmvD-d33Rvt59PM9NipnW4rFhxSLrXAFnZp8OOLPn7CJ01QZZ1VZks1ruV1-q3SsqwyO6V7NPk_5DXrlVMj27fM8Qz8vv9xdXDc3t1dfL85vGsOZKA0b3DgKBZ0bNOUATNHOKWqcrV9qEK6n42C54hQGAk5vOTFAhNKaE73tBnaGPjz11mP_LDYXOfm8vqlmG5csSc8EHwTdbmuUPkVNijkn6-Qh-aleLgnIVYrcy1WKXKVIELJKqdD75_5FT3b8j_yzwB4B3D-MQw</recordid><startdate>20141024</startdate><enddate>20141024</enddate><creator>Lee, Asaka</creator><creator>Asahina, Kota</creator><creator>Okamoto, Takumi</creator><creator>Kawaguchi, Kosuke</creator><creator>Kostsin, Dzmitry G</creator><creator>Kashiwayama, Yoshinori</creator><creator>Takanashi, Kojiro</creator><creator>Yazaki, Kazufumi</creator><creator>Imanaka, Tsuneo</creator><creator>Morita, Masashi</creator><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>20141024</creationdate><title>Role of NH2-terminal hydrophobic motif in the subcellular localization of ATP-binding cassette protein subfamily D: common features in eukaryotic organisms</title><author>Lee, Asaka ; Asahina, Kota ; Okamoto, Takumi ; Kawaguchi, Kosuke ; Kostsin, Dzmitry G ; Kashiwayama, Yoshinori ; Takanashi, Kojiro ; Yazaki, Kazufumi ; Imanaka, Tsuneo ; Morita, Masashi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c439t-38fdd9a05f8b24003a25fa2cfe530b09f62d8e4a420810fb741c019abb41b7583</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Animals</topic><topic>Arabidopsis - metabolism</topic><topic>ATP-Binding Cassette Transporters - chemistry</topic><topic>ATP-Binding Cassette Transporters - metabolism</topic><topic>Caenorhabditis elegans - metabolism</topic><topic>CHO Cells</topic><topic>Cricetinae</topic><topic>Cricetulus</topic><topic>Eukaryotic Cells - metabolism</topic><topic>Fluorescent Antibody Technique</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>Subcellular Fractions - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lee, Asaka</creatorcontrib><creatorcontrib>Asahina, Kota</creatorcontrib><creatorcontrib>Okamoto, Takumi</creatorcontrib><creatorcontrib>Kawaguchi, Kosuke</creatorcontrib><creatorcontrib>Kostsin, Dzmitry G</creatorcontrib><creatorcontrib>Kashiwayama, Yoshinori</creatorcontrib><creatorcontrib>Takanashi, Kojiro</creatorcontrib><creatorcontrib>Yazaki, Kazufumi</creatorcontrib><creatorcontrib>Imanaka, Tsuneo</creatorcontrib><creatorcontrib>Morita, Masashi</creatorcontrib><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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lee, Asaka</au><au>Asahina, Kota</au><au>Okamoto, Takumi</au><au>Kawaguchi, Kosuke</au><au>Kostsin, Dzmitry G</au><au>Kashiwayama, Yoshinori</au><au>Takanashi, Kojiro</au><au>Yazaki, Kazufumi</au><au>Imanaka, Tsuneo</au><au>Morita, Masashi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Role of NH2-terminal hydrophobic motif in the subcellular localization of ATP-binding cassette protein subfamily D: common features in eukaryotic organisms</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2014-10-24</date><risdate>2014</risdate><volume>453</volume><issue>3</issue><spage>612</spage><epage>618</epage><pages>612-618</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>In mammals, four ATP-binding cassette (ABC) proteins belonging to subfamily D have been identified. ABCD1-3 possesses the NH2-terminal hydrophobic region and are targeted to peroxisomes, while ABCD4 lacking the region is targeted to the endoplasmic reticulum (ER). Based on hydropathy plot analysis, we found that several eukaryotes have ABCD protein homologs lacking the NH2-terminal hydrophobic segment (H0 motif). To investigate whether the role of the NH2-terminal H0 motif in subcellular localization is conserved across species, we expressed ABCD proteins from several species (metazoan, plant and fungi) in fusion with GFP in CHO cells and examined their subcellular localization. ABCD proteins possessing the NH2-terminal H0 motif were localized to peroxisomes, while ABCD proteins lacking this region lost this capacity. In addition, the deletion of the NH2-terminal H0 motif of ABCD protein resulted in their localization to the ER. These results suggest that the role of the NH2-terminal H0 motif in organelle targeting is widely conserved in living organisms.</abstract><cop>United States</cop><pmid>25301552</pmid><doi>10.1016/j.bbrc.2014.09.133</doi><tpages>7</tpages></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Animals Arabidopsis - metabolism ATP-Binding Cassette Transporters - chemistry ATP-Binding Cassette Transporters - metabolism Caenorhabditis elegans - metabolism CHO Cells Cricetinae Cricetulus Eukaryotic Cells - metabolism Fluorescent Antibody Technique Hydrophobic and Hydrophilic Interactions Subcellular Fractions - metabolism |
| title | Role of NH2-terminal hydrophobic motif in the subcellular localization of ATP-binding cassette protein subfamily D: common features in eukaryotic organisms |
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