Arabidopsis μA-adaptin interacts with the tyrosine motif of the vacuolar sorting receptor VSR-PS1
In receptor-mediated transport pathways in mammalian cells, clathrin-coated vesicle (CCV) mu-adaptins are the main binding partners for the tyrosine sorting/internalization motif (YXXØ). We have analyzed the function of the mu A-adaptin, one of the five mu-adaptins from Arabidopsis thaliana, by pull...
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| Veröffentlicht in: | The Plant journal : for cell and molecular biology 2004-03, Vol.37 (5), p.678-693 |
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| container_title | The Plant journal : for cell and molecular biology |
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| creator | HAPPEL, Nicole HÖNING, Stefan NEUHAUS, Jean-Marc PARIS, Nadine ROBINSON, David G HOLSTEIN, Susanne E. H |
| description | In receptor-mediated transport pathways in mammalian cells, clathrin-coated vesicle (CCV) mu-adaptins are the main binding partners for the tyrosine sorting/internalization motif (YXXØ). We have analyzed the function of the mu A-adaptin, one of the five mu-adaptins from Arabidopsis thaliana, by pull-down assays and plasmon resonance measurements using its receptor-binding domain (RBD) fused to a histidine tag. We show that this adaptin is able to bind the consensus tyrosine motif YXXØ from the pea vacuolar sorting receptor (VSR)-PS1, as well as from the mammalian trans-Golgi network (TGN)38 protein. Moreover, the tyrosine residue was revealed to be crucial for binding of the complete cytoplasmic tail of VSR-PS1 to the plant mu A-adaptin. The trans-Golgi localization of the mu A-adaptin strongly suggests its involvement in Golgi- to vacuole-trafficking events. |
| doi_str_mv | 10.1111/j.1365-313X.2003.01995.x |
| format | Article |
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The trans-Golgi localization of the mu A-adaptin strongly suggests its involvement in Golgi- to vacuole-trafficking events.</description><identifier>ISSN: 0960-7412</identifier><identifier>EISSN: 1365-313X</identifier><identifier>DOI: 10.1111/j.1365-313X.2003.01995.x</identifier><identifier>PMID: 14871308</identifier><language>eng</language><publisher>Oxford: Blackwell Science</publisher><subject>Adaptor Protein Complex mu Subunits - genetics ; Adaptor Protein Complex mu Subunits - metabolism ; Amino Acid Sequence ; Arabidopsis - genetics ; Arabidopsis - metabolism ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - metabolism ; Biological and medical sciences ; Cell physiology ; DNA, Complementary - chemistry ; DNA, Complementary - genetics ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation, Plant ; Golgi Apparatus - metabolism ; Molecular Sequence Data ; Plant physiology and development ; Plasma membrane and permeation ; Protein Transport ; Sequence Analysis, DNA ; Sequence Homology, Amino Acid ; Tyrosine - genetics ; Tyrosine - metabolism ; Vacuoles - metabolism ; Vesicular Transport Proteins - genetics ; Vesicular Transport Proteins - metabolism</subject><ispartof>The Plant journal : for cell and molecular biology, 2004-03, Vol.37 (5), p.678-693</ispartof><rights>2004 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15514230$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14871308$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>HAPPEL, Nicole</creatorcontrib><creatorcontrib>HÖNING, Stefan</creatorcontrib><creatorcontrib>NEUHAUS, Jean-Marc</creatorcontrib><creatorcontrib>PARIS, Nadine</creatorcontrib><creatorcontrib>ROBINSON, David G</creatorcontrib><creatorcontrib>HOLSTEIN, Susanne E. H</creatorcontrib><title>Arabidopsis μA-adaptin interacts with the tyrosine motif of the vacuolar sorting receptor VSR-PS1</title><title>The Plant journal : for cell and molecular biology</title><addtitle>Plant J</addtitle><description>In receptor-mediated transport pathways in mammalian cells, clathrin-coated vesicle (CCV) mu-adaptins are the main binding partners for the tyrosine sorting/internalization motif (YXXØ). We have analyzed the function of the mu A-adaptin, one of the five mu-adaptins from Arabidopsis thaliana, by pull-down assays and plasmon resonance measurements using its receptor-binding domain (RBD) fused to a histidine tag. We show that this adaptin is able to bind the consensus tyrosine motif YXXØ from the pea vacuolar sorting receptor (VSR)-PS1, as well as from the mammalian trans-Golgi network (TGN)38 protein. Moreover, the tyrosine residue was revealed to be crucial for binding of the complete cytoplasmic tail of VSR-PS1 to the plant mu A-adaptin. The trans-Golgi localization of the mu A-adaptin strongly suggests its involvement in Golgi- to vacuole-trafficking events.</description><subject>Adaptor Protein Complex mu Subunits - genetics</subject><subject>Adaptor Protein Complex mu Subunits - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis - metabolism</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>Biological and medical sciences</subject><subject>Cell physiology</subject><subject>DNA, Complementary - chemistry</subject><subject>DNA, Complementary - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation, Plant</subject><subject>Golgi Apparatus - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Plant physiology and development</subject><subject>Plasma membrane and permeation</subject><subject>Protein Transport</subject><subject>Sequence Analysis, DNA</subject><subject>Sequence Homology, Amino Acid</subject><subject>Tyrosine - genetics</subject><subject>Tyrosine - metabolism</subject><subject>Vacuoles - metabolism</subject><subject>Vesicular Transport Proteins - genetics</subject><subject>Vesicular Transport Proteins - metabolism</subject><issn>0960-7412</issn><issn>1365-313X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkE1OwzAQRi0EoqVwBeQN7BLs2I7jZVXxJ1UCUUDsIttxqKs0DrYD9G6cgTMRQYHZfNJ8b2bxAIAYpXiYs1WKSc4SgslTmiFEUoSFYOn7Dhj_FbtgjESOEk5xNgIHIawQwpzkdB-MMC04JqgYAzX1UtnKdcEG-PkxTWQlu2hbaNtovNQxwDcblzAuDYwb74JtDVy7aGvo6u_tq9S9a6SHwfnh8Bl6o00XnYePi7vkdoEPwV4tm2COtjkBDxfn97OrZH5zeT2bzpMuIzwmEueE55RkOaUVN6hgWBeVYizXjBItqqwqhNIKI25ojjgWmismqKqFYrJiZAJOf_523r30JsRybYM2TSNb4_pQFghTQQdbE3C8BXu1NlXZebuWflP-WhmAky0gg5ZN7WWrbfjnGMM0I4h8AYiFc64</recordid><startdate>20040301</startdate><enddate>20040301</enddate><creator>HAPPEL, Nicole</creator><creator>HÖNING, Stefan</creator><creator>NEUHAUS, Jean-Marc</creator><creator>PARIS, Nadine</creator><creator>ROBINSON, David G</creator><creator>HOLSTEIN, Susanne E. 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Psychology</topic><topic>Gene Expression Regulation, Plant</topic><topic>Golgi Apparatus - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Plant physiology and development</topic><topic>Plasma membrane and permeation</topic><topic>Protein Transport</topic><topic>Sequence Analysis, DNA</topic><topic>Sequence Homology, Amino Acid</topic><topic>Tyrosine - genetics</topic><topic>Tyrosine - metabolism</topic><topic>Vacuoles - metabolism</topic><topic>Vesicular Transport Proteins - genetics</topic><topic>Vesicular Transport Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>HAPPEL, Nicole</creatorcontrib><creatorcontrib>HÖNING, Stefan</creatorcontrib><creatorcontrib>NEUHAUS, Jean-Marc</creatorcontrib><creatorcontrib>PARIS, Nadine</creatorcontrib><creatorcontrib>ROBINSON, David G</creatorcontrib><creatorcontrib>HOLSTEIN, Susanne E. 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We show that this adaptin is able to bind the consensus tyrosine motif YXXØ from the pea vacuolar sorting receptor (VSR)-PS1, as well as from the mammalian trans-Golgi network (TGN)38 protein. Moreover, the tyrosine residue was revealed to be crucial for binding of the complete cytoplasmic tail of VSR-PS1 to the plant mu A-adaptin. The trans-Golgi localization of the mu A-adaptin strongly suggests its involvement in Golgi- to vacuole-trafficking events.</abstract><cop>Oxford</cop><pub>Blackwell Science</pub><pmid>14871308</pmid><doi>10.1111/j.1365-313X.2003.01995.x</doi><tpages>16</tpages></addata></record> |
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| subjects | Adaptor Protein Complex mu Subunits - genetics Adaptor Protein Complex mu Subunits - metabolism Amino Acid Sequence Arabidopsis - genetics Arabidopsis - metabolism Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Biological and medical sciences Cell physiology DNA, Complementary - chemistry DNA, Complementary - genetics Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Plant Golgi Apparatus - metabolism Molecular Sequence Data Plant physiology and development Plasma membrane and permeation Protein Transport Sequence Analysis, DNA Sequence Homology, Amino Acid Tyrosine - genetics Tyrosine - metabolism Vacuoles - metabolism Vesicular Transport Proteins - genetics Vesicular Transport Proteins - metabolism |
| title | Arabidopsis μA-adaptin interacts with the tyrosine motif of the vacuolar sorting receptor VSR-PS1 |
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