{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T07:12:32Z","timestamp":1790925152795,"version":"4.1.0"},"reference-count":47,"publisher":"The Company of Biologists","issue":"6","license":[{"start":{"date-parts":[[2024,3,21]],"date-time":"2024-03-21T00:00:00Z","timestamp":1710979200000},"content-version":"vor","delay-in-days":6,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/100007890","name":"University of North Carolina at Chapel Hill","doi-asserted-by":"crossref","id":[{"id":"10.13039\/100007890","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["R15 GM114729"],"award-info":[{"award-number":["R15 GM114729"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["R35 GM118096"],"award-info":[{"award-number":["R35 GM118096"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2024,3,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n               <jats:p>Robust linkage between adherens junctions and the actomyosin cytoskeleton allows cells to change shape and move during morphogenesis without tearing tissues apart. The Drosophila multidomain protein Canoe and its mammalian homolog afadin are crucial for this, as in their absence many events of morphogenesis fail. To define the mechanism of action for Canoe, we are taking it apart. Canoe has five folded protein domains and a long intrinsically disordered region. The largest is the Dilute domain, which is shared by Canoe and myosin V. To define the roles of this domain in Canoe, we combined biochemical, genetic and cell biological assays. AlphaFold was used to predict its structure, providing similarities and contrasts with Myosin V. Biochemical data suggested one potential shared function \u2013 the ability to dimerize. We generated Canoe mutants with the Dilute domain deleted (Cno\u0394DIL). Surprisingly, they were viable and fertile. Cno\u0394DIL localized to adherens junctions and was enriched at junctions under tension. However, when its dose was reduced, Cno\u0394DIL did not provide fully wild-type function. Furthermore, canoe\u0394DIL mutants had defects in the orchestrated cell rearrangements of eye development. This reveals the robustness of junction\u2013cytoskeletal connections during morphogenesis and highlights the power of natural selection to maintain protein structure.<\/jats:p>","DOI":"10.1242\/jcs.261734","type":"journal-article","created":{"date-parts":[[2024,2,7]],"date-time":"2024-02-07T15:18:34Z","timestamp":1707319114000},"source":"Crossref","is-referenced-by-count":9,"title":["The Dilute domain in Canoe is not essential for linking cell junctions to the cytoskeleton but supports morphogenesis robustness"],"prefix":"10.1242","volume":"137","author":[{"ORCID":"https:\/\/orcid.org\/0009-0002-6164-243X","authenticated-orcid":false,"given":"Emily D.","family":"McParland","sequence":"first","affiliation":[{"name":"University of North Carolina at Chapel Hill 1 Department of Biology , , CB#3280, Chapel Hill, NC 27599-3280 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"T. Amber","family":"Butcher","sequence":"additional","affiliation":[{"name":"University of North Carolina at Chapel Hill 1 Department of Biology , , CB#3280, Chapel Hill, NC 27599-3280 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Noah J.","family":"Gurley","sequence":"additional","affiliation":[{"name":"University of North Carolina at Chapel Hill 1 Department of Biology , , CB#3280, Chapel Hill, NC 27599-3280 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ruth I.","family":"Johnson","sequence":"additional","affiliation":[{"name":"Wesleyan University 2 Biology Department , , Middletown, CT 06459 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kevin C.","family":"Slep","sequence":"additional","affiliation":[{"name":"University of North Carolina at Chapel Hill 1 Department of Biology , , CB#3280, Chapel Hill, NC 27599-3280 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1412-3987","authenticated-orcid":false,"given":"Mark","family":"Peifer","sequence":"additional","affiliation":[{"name":"University of North Carolina at Chapel Hill 1 Department of Biology , , CB#3280, Chapel Hill, NC 27599-3280 , USA"},{"name":"Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill 3 , Chapel Hill, NC 27599 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","published-online":{"date-parts":[[2024,3,21]]},"reference":[{"key":"2024040812434772300_JCS261734C1","doi-asserted-by":"publisher","first-page":"4103","DOI":"10.1074\/jbc.M209832200","article-title":"ADIP, a novel Afadin- and \u03b1-actinin-binding protein localized at cell-cell adherens junctions","volume":"278","author":"Asada","year":"2003","journal-title":"J. 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