Sumoylation in axons triggers retrograde transport of the RNA-binding protein La
A surprisingly large population of mRNAs has been shown to localize to sensory axons, but few RNA-binding proteins have been detected in these axons. These axonal mRNAs include several potential binding targets for the La RNA chaperone protein. La is transported into axonal processes in both culture...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2007-07, Vol.104 (31), p.12913-12918 |
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creator | van Niekerk, Erna A Willis, Dianna E Chang, Jay H Reumann, Kerstin Heise, Tilman Twiss, Jeffery L |
description | A surprisingly large population of mRNAs has been shown to localize to sensory axons, but few RNA-binding proteins have been detected in these axons. These axonal mRNAs include several potential binding targets for the La RNA chaperone protein. La is transported into axonal processes in both culture and peripheral nerve. Interestingly, La is posttranslationally modified in sensory neurons by sumoylation. In axons, small ubiquitin-like modifying polypeptides (SUMO)-La interacts with dynein, whereas native La interacts with kinesin. Lysine 41 is required for sumoylation, and sumoylation-incompetent LaK⁴¹R shows only anterograde transport, whereas WT La shows both anterograde and retrograde transport in axons. Thus, sumoylation of La determines the directionality of its transport within the axonal compartment, with SUMO-La likely recycling to the cell body. |
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These axonal mRNAs include several potential binding targets for the La RNA chaperone protein. La is transported into axonal processes in both culture and peripheral nerve. Interestingly, La is posttranslationally modified in sensory neurons by sumoylation. In axons, small ubiquitin-like modifying polypeptides (SUMO)-La interacts with dynein, whereas native La interacts with kinesin. Lysine 41 is required for sumoylation, and sumoylation-incompetent LaK⁴¹R shows only anterograde transport, whereas WT La shows both anterograde and retrograde transport in axons. Thus, sumoylation of La determines the directionality of its transport within the axonal compartment, with SUMO-La likely recycling to the cell body.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0611562104</identifier><identifier>PMID: 17646655</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Animals ; Antibodies ; Autoantigens - genetics ; Autoantigens - metabolism ; Axonal Transport ; Axons ; Axons - metabolism ; Binding sites ; Biological Sciences ; Cell culture ; Dyneins - metabolism ; Humans ; Kinesin - metabolism ; Ligation ; Messenger RNA ; Mucoproteins - genetics ; Mucoproteins - metabolism ; Mutation - genetics ; Neurons ; PC12 cells ; Peptides ; Protein Binding ; Protein Transport ; Proteins ; Rats ; Rats, Sprague-Dawley ; Ribonucleic acid ; RNA ; RNA binding proteins ; RNA, Messenger - genetics ; RNA-Binding Proteins - genetics ; RNA-Binding Proteins - metabolism ; Sciatic nerve ; Sciatic Nerve - metabolism ; SUMO-1 Protein - metabolism ; Tissue Culture Techniques</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2007-07, Vol.104 (31), p.12913-12918</ispartof><rights>Copyright 2007 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Jul 31, 2007</rights><rights>2007 by The National Academy of Sciences of the USA 2007</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c620t-61e58c21eaee66c6fcb6d71393c0e734049a70a4b61134c84d4853c66ca90dd93</citedby><cites>FETCH-LOGICAL-c620t-61e58c21eaee66c6fcb6d71393c0e734049a70a4b61134c84d4853c66ca90dd93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/104/31.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/25436404$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/25436404$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,315,729,782,786,805,887,27933,27934,53800,53802,58026,58259</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17646655$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>van Niekerk, Erna A</creatorcontrib><creatorcontrib>Willis, Dianna E</creatorcontrib><creatorcontrib>Chang, Jay H</creatorcontrib><creatorcontrib>Reumann, Kerstin</creatorcontrib><creatorcontrib>Heise, Tilman</creatorcontrib><creatorcontrib>Twiss, Jeffery L</creatorcontrib><title>Sumoylation in axons triggers retrograde transport of the RNA-binding protein La</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>A surprisingly large population of mRNAs has been shown to localize to sensory axons, but few RNA-binding proteins have been detected in these axons. These axonal mRNAs include several potential binding targets for the La RNA chaperone protein. La is transported into axonal processes in both culture and peripheral nerve. Interestingly, La is posttranslationally modified in sensory neurons by sumoylation. In axons, small ubiquitin-like modifying polypeptides (SUMO)-La interacts with dynein, whereas native La interacts with kinesin. Lysine 41 is required for sumoylation, and sumoylation-incompetent LaK⁴¹R shows only anterograde transport, whereas WT La shows both anterograde and retrograde transport in axons. Thus, sumoylation of La determines the directionality of its transport within the axonal compartment, with SUMO-La likely recycling to the cell body.</description><subject>Animals</subject><subject>Antibodies</subject><subject>Autoantigens - genetics</subject><subject>Autoantigens - metabolism</subject><subject>Axonal Transport</subject><subject>Axons</subject><subject>Axons - metabolism</subject><subject>Binding sites</subject><subject>Biological Sciences</subject><subject>Cell culture</subject><subject>Dyneins - metabolism</subject><subject>Humans</subject><subject>Kinesin - metabolism</subject><subject>Ligation</subject><subject>Messenger RNA</subject><subject>Mucoproteins - genetics</subject><subject>Mucoproteins - metabolism</subject><subject>Mutation - genetics</subject><subject>Neurons</subject><subject>PC12 cells</subject><subject>Peptides</subject><subject>Protein Binding</subject><subject>Protein Transport</subject><subject>Proteins</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>RNA binding proteins</subject><subject>RNA, Messenger - genetics</subject><subject>RNA-Binding Proteins - genetics</subject><subject>RNA-Binding Proteins - metabolism</subject><subject>Sciatic nerve</subject><subject>Sciatic Nerve - metabolism</subject><subject>SUMO-1 Protein - metabolism</subject><subject>Tissue Culture Techniques</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1v1DAQxS0EosvCmRMQcUDikHb8kUl8QaoqvqQVIErPltdx0qyy9mI7qP3vcdhVF7j0ZMnzm6f35hHynMIphZqf7ZyOp4CUVsgoiAdkQUHSEoWEh2QBwOqyEUyckCcxbgBAVg08Jie0RoFYVQvy7XLa-ttRp8G7YnCFvvEuFikMfW9DLIJNwfdBtzb_aRd3PqTCd0W6tsX3L-flenDt4PpiF3yyeX2ln5JHnR6jfXZ4l-Tqw_sfF5_K1dePny_OV6VBBqlEaqvGMGq1tYgGO7PGtqZccgO25gKE1DVosc7ZuDCNaEVTcZNRLaFtJV-Sd3vd3bTe2tZYlw2OaheGrQ63yutB_Ttxw7Xq_S9FJa8rxCzw5iAQ_M_JxqS2QzR2HLWzfooKG0oRa7gXZFChBD5bev0fuPFTcPkKmaGc8RlbkrM9ZIKPMdjuzjIFNXeq5k7VsdO88fLvpEf-UGIG3h6AefMoJxSnijJJueqmcUz2JmW2uIfNyIs9sonJhzuGVYKj-OPn1X7eaa90H4aori7ngAC1FBIZ_w15kMio</recordid><startdate>20070731</startdate><enddate>20070731</enddate><creator>van Niekerk, Erna A</creator><creator>Willis, Dianna E</creator><creator>Chang, Jay H</creator><creator>Reumann, Kerstin</creator><creator>Heise, Tilman</creator><creator>Twiss, Jeffery L</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>FBQ</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7ST</scope><scope>7U6</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20070731</creationdate><title>Sumoylation in axons triggers retrograde transport of the RNA-binding protein La</title><author>van Niekerk, Erna A ; 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subjects | Animals Antibodies Autoantigens - genetics Autoantigens - metabolism Axonal Transport Axons Axons - metabolism Binding sites Biological Sciences Cell culture Dyneins - metabolism Humans Kinesin - metabolism Ligation Messenger RNA Mucoproteins - genetics Mucoproteins - metabolism Mutation - genetics Neurons PC12 cells Peptides Protein Binding Protein Transport Proteins Rats Rats, Sprague-Dawley Ribonucleic acid RNA RNA binding proteins RNA, Messenger - genetics RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism Sciatic nerve Sciatic Nerve - metabolism SUMO-1 Protein - metabolism Tissue Culture Techniques |
title | Sumoylation in axons triggers retrograde transport of the RNA-binding protein La |
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