Dynamin-1-like protein (Dnm1L) interaction with kinesin light chain 1 (KLC1) through the tetratricopeptide repeat (TPR) domains
Kinesin light chain 1 (KLC1) mediates binding of KIF5 motor to specific cargo. Using the yeast two-hybrid screening, we found that mitochondrial fission protein dynamin-1-like protein (Dnm1L) interacted with KLC1, but not KIF5. Dnm1L and KLC1 were co-localized in cultured cells. These results sugges...
Gespeichert in:
| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2014-12, Vol.78 (12), p.2069-2072 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 2072 |
|---|---|
| container_issue | 12 |
| container_start_page | 2069 |
| container_title | Bioscience, biotechnology, and biochemistry |
| container_volume | 78 |
| creator | Jang, Won Hee Jeong, Young Joo Choi, Sun Hee Kim, Sang-Jin Urm, Sang-Hwa Seog, Dae-Hyun |
| description | Kinesin light chain 1 (KLC1) mediates binding of KIF5 motor to specific cargo. Using the yeast two-hybrid screening, we found that mitochondrial fission protein dynamin-1-like protein (Dnm1L) interacted with KLC1, but not KIF5. Dnm1L and KLC1 were co-localized in cultured cells. These results suggest that KLC1 may play a potential role in post-fission mitochondrial transport. |
| doi_str_mv | 10.1080/09168451.2014.943652 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmed_primary_25082190</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><oup_id>10.1080/09168451.2014.943652</oup_id><sourcerecordid>1629584682</sourcerecordid><originalsourceid>FETCH-LOGICAL-c473t-4f13a92d609aa59db314f64a1a08523c2f44362ebc6f2504cdf102496314b76e3</originalsourceid><addsrcrecordid>eNqNkM1u1DAURi0EokPhDRDycmaRqa_jeOIVQlP-xEggVNaWx7Eb08QOtqNqVrw6HqVliVjdK-t8n3UPQq-BbIG05IoI4C1rYEsJsK1gNW_oE7SCmu0qLtjuKVqdkerMXKAXKf0kpDw08Bxd0Ia0FARZod_XJ69G5yuoBndn8BRDNs7j9bUf4bDBzmcTlc4ueHzvco_vnDepAIO77TPWvSo74PWXwx42OPcxzLd9mQZnk6PK0ekwmSm7zuBoJqMyXt98-77BXRhLNL1Ez6waknn1MC_Rjw_vb_afqsPXj5_37w6VZrs6V8xCrQTtOBFKNaI71sAsZwoUaRtaa2pZEUDNUXNbjmO6s0AoE7xwxx039SVaL73lwF-zSVmOLmkzDMqbMCcJnIqmZbylBWULqmNIKRorp-hGFU8SiDyrl4_q5Vm9XNSX2JuHH-bjaLq_oUfXBbhagDBP_1v5dkk4b0Mc1X2IQyezOg0h2qi8dknW_2z4Ayy4nqI</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1629584682</pqid></control><display><type>article</type><title>Dynamin-1-like protein (Dnm1L) interaction with kinesin light chain 1 (KLC1) through the tetratricopeptide repeat (TPR) domains</title><source>MEDLINE</source><source>Oxford University Press Journals All Titles (1996-Current)</source><source>Freely Accessible Japanese Titles</source><source>EZB-FREE-00999 freely available EZB journals</source><creator>Jang, Won Hee ; Jeong, Young Joo ; Choi, Sun Hee ; Kim, Sang-Jin ; Urm, Sang-Hwa ; Seog, Dae-Hyun</creator><creatorcontrib>Jang, Won Hee ; Jeong, Young Joo ; Choi, Sun Hee ; Kim, Sang-Jin ; Urm, Sang-Hwa ; Seog, Dae-Hyun</creatorcontrib><description>Kinesin light chain 1 (KLC1) mediates binding of KIF5 motor to specific cargo. Using the yeast two-hybrid screening, we found that mitochondrial fission protein dynamin-1-like protein (Dnm1L) interacted with KLC1, but not KIF5. Dnm1L and KLC1 were co-localized in cultured cells. These results suggest that KLC1 may play a potential role in post-fission mitochondrial transport.</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1080/09168451.2014.943652</identifier><identifier>PMID: 25082190</identifier><language>eng</language><publisher>England: Taylor & Francis</publisher><subject>Binding Sites ; Biological Transport ; Dnm1L ; Gene Expression Regulation ; GTP Phosphohydrolases - genetics ; GTP Phosphohydrolases - metabolism ; HEK293 Cells ; Humans ; Kinesin - genetics ; Kinesin - metabolism ; kinesin 1 ; KLC1 ; Microtubule-Associated Proteins - genetics ; Microtubule-Associated Proteins - metabolism ; Mitochondria - genetics ; Mitochondria - metabolism ; Mitochondrial Dynamics - genetics ; Mitochondrial Proteins - genetics ; Mitochondrial Proteins - metabolism ; Protein Binding ; Protein Structure, Tertiary ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Signal Transduction ; TPR domain ; Two-Hybrid System Techniques</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2014-12, Vol.78 (12), p.2069-2072</ispartof><rights>2014 Japan Society for Bioscience, Biotechnology, and Agrochemistry 2014</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c473t-4f13a92d609aa59db314f64a1a08523c2f44362ebc6f2504cdf102496314b76e3</citedby><cites>FETCH-LOGICAL-c473t-4f13a92d609aa59db314f64a1a08523c2f44362ebc6f2504cdf102496314b76e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25082190$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jang, Won Hee</creatorcontrib><creatorcontrib>Jeong, Young Joo</creatorcontrib><creatorcontrib>Choi, Sun Hee</creatorcontrib><creatorcontrib>Kim, Sang-Jin</creatorcontrib><creatorcontrib>Urm, Sang-Hwa</creatorcontrib><creatorcontrib>Seog, Dae-Hyun</creatorcontrib><title>Dynamin-1-like protein (Dnm1L) interaction with kinesin light chain 1 (KLC1) through the tetratricopeptide repeat (TPR) domains</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>Kinesin light chain 1 (KLC1) mediates binding of KIF5 motor to specific cargo. Using the yeast two-hybrid screening, we found that mitochondrial fission protein dynamin-1-like protein (Dnm1L) interacted with KLC1, but not KIF5. Dnm1L and KLC1 were co-localized in cultured cells. These results suggest that KLC1 may play a potential role in post-fission mitochondrial transport.</description><subject>Binding Sites</subject><subject>Biological Transport</subject><subject>Dnm1L</subject><subject>Gene Expression Regulation</subject><subject>GTP Phosphohydrolases - genetics</subject><subject>GTP Phosphohydrolases - metabolism</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>Kinesin - genetics</subject><subject>Kinesin - metabolism</subject><subject>kinesin 1</subject><subject>KLC1</subject><subject>Microtubule-Associated Proteins - genetics</subject><subject>Microtubule-Associated Proteins - metabolism</subject><subject>Mitochondria - genetics</subject><subject>Mitochondria - metabolism</subject><subject>Mitochondrial Dynamics - genetics</subject><subject>Mitochondrial Proteins - genetics</subject><subject>Mitochondrial Proteins - metabolism</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Signal Transduction</subject><subject>TPR domain</subject><subject>Two-Hybrid System Techniques</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkM1u1DAURi0EokPhDRDycmaRqa_jeOIVQlP-xEggVNaWx7Eb08QOtqNqVrw6HqVliVjdK-t8n3UPQq-BbIG05IoI4C1rYEsJsK1gNW_oE7SCmu0qLtjuKVqdkerMXKAXKf0kpDw08Bxd0Ia0FARZod_XJ69G5yuoBndn8BRDNs7j9bUf4bDBzmcTlc4ueHzvco_vnDepAIO77TPWvSo74PWXwx42OPcxzLd9mQZnk6PK0ekwmSm7zuBoJqMyXt98-77BXRhLNL1Ez6waknn1MC_Rjw_vb_afqsPXj5_37w6VZrs6V8xCrQTtOBFKNaI71sAsZwoUaRtaa2pZEUDNUXNbjmO6s0AoE7xwxx039SVaL73lwF-zSVmOLmkzDMqbMCcJnIqmZbylBWULqmNIKRorp-hGFU8SiDyrl4_q5Vm9XNSX2JuHH-bjaLq_oUfXBbhagDBP_1v5dkk4b0Mc1X2IQyezOg0h2qi8dknW_2z4Ayy4nqI</recordid><startdate>20141202</startdate><enddate>20141202</enddate><creator>Jang, Won Hee</creator><creator>Jeong, Young Joo</creator><creator>Choi, Sun Hee</creator><creator>Kim, Sang-Jin</creator><creator>Urm, Sang-Hwa</creator><creator>Seog, Dae-Hyun</creator><general>Taylor & Francis</general><general>Oxford 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>7X8</scope></search><sort><creationdate>20141202</creationdate><title>Dynamin-1-like protein (Dnm1L) interaction with kinesin light chain 1 (KLC1) through the tetratricopeptide repeat (TPR) domains</title><author>Jang, Won Hee ; Jeong, Young Joo ; Choi, Sun Hee ; Kim, Sang-Jin ; Urm, Sang-Hwa ; Seog, Dae-Hyun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c473t-4f13a92d609aa59db314f64a1a08523c2f44362ebc6f2504cdf102496314b76e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Binding Sites</topic><topic>Biological Transport</topic><topic>Dnm1L</topic><topic>Gene Expression Regulation</topic><topic>GTP Phosphohydrolases - genetics</topic><topic>GTP Phosphohydrolases - metabolism</topic><topic>HEK293 Cells</topic><topic>Humans</topic><topic>Kinesin - genetics</topic><topic>Kinesin - metabolism</topic><topic>kinesin 1</topic><topic>KLC1</topic><topic>Microtubule-Associated Proteins - genetics</topic><topic>Microtubule-Associated Proteins - metabolism</topic><topic>Mitochondria - genetics</topic><topic>Mitochondria - metabolism</topic><topic>Mitochondrial Dynamics - genetics</topic><topic>Mitochondrial Proteins - genetics</topic><topic>Mitochondrial Proteins - metabolism</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Signal Transduction</topic><topic>TPR domain</topic><topic>Two-Hybrid System Techniques</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jang, Won Hee</creatorcontrib><creatorcontrib>Jeong, Young Joo</creatorcontrib><creatorcontrib>Choi, Sun Hee</creatorcontrib><creatorcontrib>Kim, Sang-Jin</creatorcontrib><creatorcontrib>Urm, Sang-Hwa</creatorcontrib><creatorcontrib>Seog, Dae-Hyun</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>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jang, Won Hee</au><au>Jeong, Young Joo</au><au>Choi, Sun Hee</au><au>Kim, Sang-Jin</au><au>Urm, Sang-Hwa</au><au>Seog, Dae-Hyun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Dynamin-1-like protein (Dnm1L) interaction with kinesin light chain 1 (KLC1) through the tetratricopeptide repeat (TPR) domains</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2014-12-02</date><risdate>2014</risdate><volume>78</volume><issue>12</issue><spage>2069</spage><epage>2072</epage><pages>2069-2072</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>Kinesin light chain 1 (KLC1) mediates binding of KIF5 motor to specific cargo. Using the yeast two-hybrid screening, we found that mitochondrial fission protein dynamin-1-like protein (Dnm1L) interacted with KLC1, but not KIF5. Dnm1L and KLC1 were co-localized in cultured cells. These results suggest that KLC1 may play a potential role in post-fission mitochondrial transport.</abstract><cop>England</cop><pub>Taylor & Francis</pub><pmid>25082190</pmid><doi>10.1080/09168451.2014.943652</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0916-8451 |
| ispartof | Bioscience, biotechnology, and biochemistry, 2014-12, Vol.78 (12), p.2069-2072 |
| issn | 0916-8451 1347-6947 |
| language | eng |
| recordid | cdi_pubmed_primary_25082190 |
| source | MEDLINE; Oxford University Press Journals All Titles (1996-Current); Freely Accessible Japanese Titles; EZB-FREE-00999 freely available EZB journals |
| subjects | Binding Sites Biological Transport Dnm1L Gene Expression Regulation GTP Phosphohydrolases - genetics GTP Phosphohydrolases - metabolism HEK293 Cells Humans Kinesin - genetics Kinesin - metabolism kinesin 1 KLC1 Microtubule-Associated Proteins - genetics Microtubule-Associated Proteins - metabolism Mitochondria - genetics Mitochondria - metabolism Mitochondrial Dynamics - genetics Mitochondrial Proteins - genetics Mitochondrial Proteins - metabolism Protein Binding Protein Structure, Tertiary Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Signal Transduction TPR domain Two-Hybrid System Techniques |
| title | Dynamin-1-like protein (Dnm1L) interaction with kinesin light chain 1 (KLC1) through the tetratricopeptide repeat (TPR) domains |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-22T10%3A40%3A26IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Dynamin-1-like%20protein%20(Dnm1L)%20interaction%20with%20kinesin%20light%20chain%201%20(KLC1)%20through%20the%20tetratricopeptide%20repeat%20(TPR)%20domains&rft.jtitle=Bioscience,%20biotechnology,%20and%20biochemistry&rft.au=Jang,%20Won%20Hee&rft.date=2014-12-02&rft.volume=78&rft.issue=12&rft.spage=2069&rft.epage=2072&rft.pages=2069-2072&rft.issn=0916-8451&rft.eissn=1347-6947&rft_id=info:doi/10.1080/09168451.2014.943652&rft_dat=%3Cproquest_pubme%3E1629584682%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1629584682&rft_id=info:pmid/25082190&rft_oup_id=10.1080/09168451.2014.943652&rfr_iscdi=true |