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Although untranslated regions (UTRs) of many different axonal <jats:styled-content style=\"fixed-case\">mRNA<\/jats:styled-content>s appear to drive their localization, there has been no consensus RNA structure responsible for this localization. We recently showed that limited expression of ZBP1 protein restricts axonal localization of both \u03b2\u2010actin and GAP\u201043 <jats:styled-content style=\"fixed-case\">mRNA<\/jats:styled-content>s. \u03b2\u2010actin 3\u2032UTR has a defined element for interaction with ZBP1, but GAP\u201043 <jats:styled-content style=\"fixed-case\">mRNA<\/jats:styled-content> shows no homology to this RNA sequence. Here, we show that an AU\u2010rich regulatory element (ARE) in GAP\u201043\u2032s 3\u2032UTR is necessary and sufficient for its axonal localization. Axonal GAP\u201043 <jats:styled-content style=\"fixed-case\">mRNA<\/jats:styled-content> levels increase after <jats:italic>in vivo<\/jats:italic> injury, and GAP\u201043 <jats:styled-content style=\"fixed-case\">mRNA<\/jats:styled-content> shows an increased half\u2010life in regenerating axons. GAP\u201043 <jats:styled-content style=\"fixed-case\">mRNA<\/jats:styled-content> interacts with both HuD and ZBP1, and HuD and ZBP1 co\u2010immunoprecipitate in an RNA\u2010dependent fashion. Reporter <jats:styled-content style=\"fixed-case\">mRNA<\/jats:styled-content> with the GAP\u201043 ARE competes with endogenous \u03b2\u2010actin <jats:styled-content style=\"fixed-case\">mRNA<\/jats:styled-content> for axonal localization and decreases axon length and branching similar to the \u03b2\u2010actin 3\u2032UTR competing with endogenous GAP\u201043 <jats:styled-content style=\"fixed-case\">mRNA<\/jats:styled-content>. Conversely, over\u2010expressing GAP\u201043 coding sequence with its 3\u2032UTR ARE increases axonal elongation and this effect is lost when just the ARE is deleted from GAP\u201043\u2032s 3\u2032UTR.<\/jats:p><jats:p>\n<jats:boxed-text content-type=\"graphic\" position=\"anchor\"><jats:graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" mimetype=\"image\/png\" position=\"anchor\" specific-use=\"enlarged-web-image\" xlink:href=\"graphic\/jnc12266-fig-0007-m.png\"><jats:alt-text>image<\/jats:alt-text><\/jats:graphic><\/jats:boxed-text>\n<\/jats:p><jats:p>We have recently found that over\u2010expression of GAP\u201043 using an axonally targeted construct with the 3\u2032UTRs of GAP\u201043 promoted elongating growth of axons, while restricting the mRNA to the cell body with the 3\u2032UTR of \u03b3\u2010actin had minimal effect on axon length. In this study, we show that the ARE in GAP\u201043\u2032s 3\u2032UTR is responsible for localization of GAP\u201043 mRNA into axons and is sufficient for GAP\u201043 protein's role in elongating axonal growth.<\/jats:p>","DOI":"10.1111\/jnc.12266","type":"journal-article","created":{"date-parts":[[2013,4,15]],"date-time":"2013-04-15T16:23:48Z","timestamp":1366043028000},"page":"792-804","source":"Crossref","is-referenced-by-count":77,"title":["A HuD\u2010ZBP1 ribonucleoprotein complex localizes GAP\u201043 <scp>mRNA<\/scp> into axons through its 3\u2032 untranslated region AU\u2010rich regulatory element"],"prefix":"10.1111","volume":"126","author":[{"given":"Soonmoon","family":"Yoo","sequence":"first","affiliation":[{"name":"Nemours Biomedical Research Alfred I. duPont Hosp. for Children Wilmington Delaware USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hak H.","family":"Kim","sequence":"additional","affiliation":[{"name":"Nemours Biomedical Research Alfred I. 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