Acyl-CoA binding domain containing 3 (ACBD3) recruits the protein phosphatase PPM1L to ER–Golgi membrane contact sites
► Acyl-CoA binding domain containing 3 (ACBD3) is an interacting partner of PPM1L. ► This association is mediated by a GOLD (Golgi dynamics) domain in ACBD3. ► ACBD3 recruits PPM1L to ER–Golgi membrane contact sites. ► ACBD3 plays a pivotal role in ceramide transport regulation. The metal-dependent...
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| Veröffentlicht in: | FEBS letters 2012-09, Vol.586 (19), p.3024-3029 |
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| creator | Shinoda, Yasuharu Fujita, Kohsuke Saito, Satoko Matsui, Hiroyuki Kanto, Yusuke Nagaura, Yuko Fukunaga, Kohji Tamura, Shinri Kobayashi, Takayasu |
| description | ► Acyl-CoA binding domain containing 3 (ACBD3) is an interacting partner of PPM1L. ► This association is mediated by a GOLD (Golgi dynamics) domain in ACBD3. ► ACBD3 recruits PPM1L to ER–Golgi membrane contact sites. ► ACBD3 plays a pivotal role in ceramide transport regulation.
The metal-dependent protein phosphatase family (PPM) governs a number of signaling pathways. PPM1L, originally identified as a negative regulator of stress-activated protein kinase signaling, was recently shown to be involved in the regulation of ceramide trafficking at ER–Golgi membrane contact sites. Here, we identified acyl-CoA binding domain containing 3 (ACBD3) as an interacting partner of PPM1L. We showed that this association, which recruits PPM1L to ER–Golgi membrane contact sites, is mediated by a GOLD (Golgi dynamics) domain in ACBD3. These results suggested that ACBD3 plays a pivotal role in ceramide transport regulation at the ER–Golgi interface.
ACBD3 and PPM1Lcolocalize by fluorescence microscopy (View interaction)
FYCO1physically interacts with PPM1L by pull down (View interaction)
SEC14L2physically interacts with PPM1L by pull down (View interaction)
ACBD3physically interacts with PPM1L by pull down (View interaction)
SEC14L1physically interacts with PPM1L by pull down (View interaction)
PPM1Lphysically interacts with ACBD3 by two hybrid (View interaction) |
| doi_str_mv | 10.1016/j.febslet.2012.06.050 |
| format | Article |
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The metal-dependent protein phosphatase family (PPM) governs a number of signaling pathways. PPM1L, originally identified as a negative regulator of stress-activated protein kinase signaling, was recently shown to be involved in the regulation of ceramide trafficking at ER–Golgi membrane contact sites. Here, we identified acyl-CoA binding domain containing 3 (ACBD3) as an interacting partner of PPM1L. We showed that this association, which recruits PPM1L to ER–Golgi membrane contact sites, is mediated by a GOLD (Golgi dynamics) domain in ACBD3. These results suggested that ACBD3 plays a pivotal role in ceramide transport regulation at the ER–Golgi interface.
ACBD3 and PPM1Lcolocalize by fluorescence microscopy (View interaction)
FYCO1physically interacts with PPM1L by pull down (View interaction)
SEC14L2physically interacts with PPM1L by pull down (View interaction)
ACBD3physically interacts with PPM1L by pull down (View interaction)
SEC14L1physically interacts with PPM1L by pull down (View interaction)
PPM1Lphysically interacts with ACBD3 by two hybrid (View interaction)</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2012.06.050</identifier><identifier>PMID: 22796112</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>ACBD3 ; acyl-CoA binding domain containing 3 ; Adaptor Proteins, Signal Transducing - chemistry ; Adaptor Proteins, Signal Transducing - genetics ; Adaptor Proteins, Signal Transducing - metabolism ; Binding Sites ; CERT ; endoplasmic reticulum ; Endoplasmic Reticulum - metabolism ; FYCO1 ; FYVE and coiled-coil domain-containing protein 1 ; GOLD ; GOLD domain ; Golgi Apparatus - metabolism ; Golgi dynamics ; HEK293 Cells ; HeLa Cells ; Humans ; Membrane Proteins - chemistry ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; metal-dependent protein phosphatase 1L ; Models, Biological ; Models, Molecular ; Phosphoprotein Phosphatases - chemistry ; Phosphoprotein Phosphatases - genetics ; Phosphoprotein Phosphatases - metabolism ; PPM1L ; Protein Interaction Domains and Motifs ; Protein Transport ; Protein-Serine-Threonine Kinases - chemistry ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; Recombinant Fusion Proteins - chemistry ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Signal Transduction ; Two-Hybrid System Techniques ; Vesicular Transport Proteins - chemistry ; Vesicular Transport Proteins - genetics ; Vesicular Transport Proteins - metabolism</subject><ispartof>FEBS letters, 2012-09, Vol.586 (19), p.3024-3029</ispartof><rights>2012 Federation of European Biochemical Societies</rights><rights>FEBS Letters 586 (2012) 2211-5463 ©2015 The Authors. Published by FEBS Press and John Wiley & Sons Ltd.</rights><rights>Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4966-2b654387de3b89f8607b6074c33612c10c579c59db7de92c0736583a762ce9143</citedby><cites>FETCH-LOGICAL-c4966-2b654387de3b89f8607b6074c33612c10c579c59db7de92c0736583a762ce9143</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2012.06.050$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.febslet.2012.06.050$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,1416,1432,3548,27923,27924,45573,45574,45994,46408,46832</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22796112$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shinoda, Yasuharu</creatorcontrib><creatorcontrib>Fujita, Kohsuke</creatorcontrib><creatorcontrib>Saito, Satoko</creatorcontrib><creatorcontrib>Matsui, Hiroyuki</creatorcontrib><creatorcontrib>Kanto, Yusuke</creatorcontrib><creatorcontrib>Nagaura, Yuko</creatorcontrib><creatorcontrib>Fukunaga, Kohji</creatorcontrib><creatorcontrib>Tamura, Shinri</creatorcontrib><creatorcontrib>Kobayashi, Takayasu</creatorcontrib><title>Acyl-CoA binding domain containing 3 (ACBD3) recruits the protein phosphatase PPM1L to ER–Golgi membrane contact sites</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>► Acyl-CoA binding domain containing 3 (ACBD3) is an interacting partner of PPM1L. ► This association is mediated by a GOLD (Golgi dynamics) domain in ACBD3. ► ACBD3 recruits PPM1L to ER–Golgi membrane contact sites. ► ACBD3 plays a pivotal role in ceramide transport regulation.
The metal-dependent protein phosphatase family (PPM) governs a number of signaling pathways. PPM1L, originally identified as a negative regulator of stress-activated protein kinase signaling, was recently shown to be involved in the regulation of ceramide trafficking at ER–Golgi membrane contact sites. Here, we identified acyl-CoA binding domain containing 3 (ACBD3) as an interacting partner of PPM1L. We showed that this association, which recruits PPM1L to ER–Golgi membrane contact sites, is mediated by a GOLD (Golgi dynamics) domain in ACBD3. These results suggested that ACBD3 plays a pivotal role in ceramide transport regulation at the ER–Golgi interface.
ACBD3 and PPM1Lcolocalize by fluorescence microscopy (View interaction)
FYCO1physically interacts with PPM1L by pull down (View interaction)
SEC14L2physically interacts with PPM1L by pull down (View interaction)
ACBD3physically interacts with PPM1L by pull down (View interaction)
SEC14L1physically interacts with PPM1L by pull down (View interaction)
PPM1Lphysically interacts with ACBD3 by two hybrid (View interaction)</description><subject>ACBD3</subject><subject>acyl-CoA binding domain containing 3</subject><subject>Adaptor Proteins, Signal Transducing - chemistry</subject><subject>Adaptor Proteins, Signal Transducing - genetics</subject><subject>Adaptor Proteins, Signal Transducing - metabolism</subject><subject>Binding Sites</subject><subject>CERT</subject><subject>endoplasmic reticulum</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>FYCO1</subject><subject>FYVE and coiled-coil domain-containing protein 1</subject><subject>GOLD</subject><subject>GOLD domain</subject><subject>Golgi Apparatus - metabolism</subject><subject>Golgi dynamics</subject><subject>HEK293 Cells</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>metal-dependent protein phosphatase 1L</subject><subject>Models, Biological</subject><subject>Models, Molecular</subject><subject>Phosphoprotein Phosphatases - chemistry</subject><subject>Phosphoprotein Phosphatases - genetics</subject><subject>Phosphoprotein Phosphatases - metabolism</subject><subject>PPM1L</subject><subject>Protein Interaction Domains and Motifs</subject><subject>Protein Transport</subject><subject>Protein-Serine-Threonine Kinases - chemistry</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Signal Transduction</subject><subject>Two-Hybrid System Techniques</subject><subject>Vesicular Transport Proteins - chemistry</subject><subject>Vesicular Transport Proteins - genetics</subject><subject>Vesicular Transport Proteins - metabolism</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc1u1DAUhS0EotPCI4C8LIuEaztxkhWaDtMfaRAVP2srce50PEriwfbQzq7vwBvyJHWUgS0srCtb3z33-FxC3jBIGTD5fpuusfEdhpQD4ynIFHJ4RmasLEQiMlk-JzMAliV5UYkTcur9FuK9ZNVLcsJ5UUnG-Iw8zPWhSxZ2ThsztGa4o63tazNQbYcQ6_gi6Pl8cfFRvKMOtdub4GnYIN05GzCSu431u00dao_09vYTW9Fg6fLL78dfV7a7M7THvnH1gJOkDtSbgP4VebGuO4-vj_WMfL9cfltcJ6vPVzeL-SrRWSVlwhuZZ6IsWhRNWa1LCUUTT6aFkIxrBjr-T-dV20Sk4hoKIfNS1IXkGiuWiTNyPulGuz_26IPqjdfYddGR3XvFolhRigxGNJ9Q7az3Dtdq50xfu0OE1Bi62qpj6GoMXYFUMfTY9_Y4Yt_02P7t-pNyBK4n4N50ePg_VXW5vOBfxw2OC2QcIM9ARqkPkxTGzH4adMprg4PG1sTlBNVa8w-3T5u4qd8</recordid><startdate>20120921</startdate><enddate>20120921</enddate><creator>Shinoda, Yasuharu</creator><creator>Fujita, Kohsuke</creator><creator>Saito, Satoko</creator><creator>Matsui, Hiroyuki</creator><creator>Kanto, Yusuke</creator><creator>Nagaura, Yuko</creator><creator>Fukunaga, Kohji</creator><creator>Tamura, Shinri</creator><creator>Kobayashi, Takayasu</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>20120921</creationdate><title>Acyl-CoA binding domain containing 3 (ACBD3) recruits the protein phosphatase PPM1L to ER–Golgi membrane contact sites</title><author>Shinoda, Yasuharu ; Fujita, Kohsuke ; Saito, Satoko ; Matsui, Hiroyuki ; Kanto, Yusuke ; Nagaura, Yuko ; Fukunaga, Kohji ; Tamura, Shinri ; Kobayashi, Takayasu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4966-2b654387de3b89f8607b6074c33612c10c579c59db7de92c0736583a762ce9143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>ACBD3</topic><topic>acyl-CoA binding domain containing 3</topic><topic>Adaptor Proteins, Signal Transducing - chemistry</topic><topic>Adaptor Proteins, Signal Transducing - genetics</topic><topic>Adaptor Proteins, Signal Transducing - metabolism</topic><topic>Binding Sites</topic><topic>CERT</topic><topic>endoplasmic reticulum</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>FYCO1</topic><topic>FYVE and coiled-coil domain-containing protein 1</topic><topic>GOLD</topic><topic>GOLD domain</topic><topic>Golgi Apparatus - metabolism</topic><topic>Golgi dynamics</topic><topic>HEK293 Cells</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>metal-dependent protein phosphatase 1L</topic><topic>Models, Biological</topic><topic>Models, Molecular</topic><topic>Phosphoprotein Phosphatases - chemistry</topic><topic>Phosphoprotein Phosphatases - genetics</topic><topic>Phosphoprotein Phosphatases - metabolism</topic><topic>PPM1L</topic><topic>Protein Interaction Domains and Motifs</topic><topic>Protein Transport</topic><topic>Protein-Serine-Threonine Kinases - chemistry</topic><topic>Protein-Serine-Threonine Kinases - genetics</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Signal Transduction</topic><topic>Two-Hybrid System Techniques</topic><topic>Vesicular Transport Proteins - chemistry</topic><topic>Vesicular Transport Proteins - genetics</topic><topic>Vesicular Transport Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shinoda, Yasuharu</creatorcontrib><creatorcontrib>Fujita, Kohsuke</creatorcontrib><creatorcontrib>Saito, Satoko</creatorcontrib><creatorcontrib>Matsui, Hiroyuki</creatorcontrib><creatorcontrib>Kanto, Yusuke</creatorcontrib><creatorcontrib>Nagaura, Yuko</creatorcontrib><creatorcontrib>Fukunaga, Kohji</creatorcontrib><creatorcontrib>Tamura, Shinri</creatorcontrib><creatorcontrib>Kobayashi, Takayasu</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>Shinoda, Yasuharu</au><au>Fujita, Kohsuke</au><au>Saito, Satoko</au><au>Matsui, Hiroyuki</au><au>Kanto, Yusuke</au><au>Nagaura, Yuko</au><au>Fukunaga, Kohji</au><au>Tamura, Shinri</au><au>Kobayashi, Takayasu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Acyl-CoA binding domain containing 3 (ACBD3) recruits the protein phosphatase PPM1L to ER–Golgi membrane contact sites</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2012-09-21</date><risdate>2012</risdate><volume>586</volume><issue>19</issue><spage>3024</spage><epage>3029</epage><pages>3024-3029</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>► Acyl-CoA binding domain containing 3 (ACBD3) is an interacting partner of PPM1L. ► This association is mediated by a GOLD (Golgi dynamics) domain in ACBD3. ► ACBD3 recruits PPM1L to ER–Golgi membrane contact sites. ► ACBD3 plays a pivotal role in ceramide transport regulation.
The metal-dependent protein phosphatase family (PPM) governs a number of signaling pathways. PPM1L, originally identified as a negative regulator of stress-activated protein kinase signaling, was recently shown to be involved in the regulation of ceramide trafficking at ER–Golgi membrane contact sites. Here, we identified acyl-CoA binding domain containing 3 (ACBD3) as an interacting partner of PPM1L. We showed that this association, which recruits PPM1L to ER–Golgi membrane contact sites, is mediated by a GOLD (Golgi dynamics) domain in ACBD3. These results suggested that ACBD3 plays a pivotal role in ceramide transport regulation at the ER–Golgi interface.
ACBD3 and PPM1Lcolocalize by fluorescence microscopy (View interaction)
FYCO1physically interacts with PPM1L by pull down (View interaction)
SEC14L2physically interacts with PPM1L by pull down (View interaction)
ACBD3physically interacts with PPM1L by pull down (View interaction)
SEC14L1physically interacts with PPM1L by pull down (View interaction)
PPM1Lphysically interacts with ACBD3 by two hybrid (View interaction)</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>22796112</pmid><doi>10.1016/j.febslet.2012.06.050</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Wiley Free Content; ScienceDirect Journals (5 years ago - present); EZB-FREE-00999 freely available EZB journals; Wiley Online Library All Journals; Alma/SFX Local Collection |
| subjects | ACBD3 acyl-CoA binding domain containing 3 Adaptor Proteins, Signal Transducing - chemistry Adaptor Proteins, Signal Transducing - genetics Adaptor Proteins, Signal Transducing - metabolism Binding Sites CERT endoplasmic reticulum Endoplasmic Reticulum - metabolism FYCO1 FYVE and coiled-coil domain-containing protein 1 GOLD GOLD domain Golgi Apparatus - metabolism Golgi dynamics HEK293 Cells HeLa Cells Humans Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism metal-dependent protein phosphatase 1L Models, Biological Models, Molecular Phosphoprotein Phosphatases - chemistry Phosphoprotein Phosphatases - genetics Phosphoprotein Phosphatases - metabolism PPM1L Protein Interaction Domains and Motifs Protein Transport Protein-Serine-Threonine Kinases - chemistry Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Signal Transduction Two-Hybrid System Techniques Vesicular Transport Proteins - chemistry Vesicular Transport Proteins - genetics Vesicular Transport Proteins - metabolism |
| title | Acyl-CoA binding domain containing 3 (ACBD3) recruits the protein phosphatase PPM1L to ER–Golgi membrane contact sites |
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