{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T00:13:13Z","timestamp":1791331993355,"version":"4.3.1"},"reference-count":49,"publisher":"Rockefeller University Press","issue":"2","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2001,7,23]]},"abstract":"<jats:p>Normal locomotion of the nematode Caenorhabditis elegans requires transmission of contractile force through a series of mechanical linkages from the myofibrillar lattice of the body wall muscles, across an intervening extracellular matrix and epithelium (the hypodermis) to the cuticle. Mutations in mua-3 cause a separation of the hypodermis from the cuticle, suggesting this gene is required for maintaining hypodermal\u2013cuticle attachment as the animal grows in size postembryonically. mua-3 encodes a predicted 3,767 amino acid protein with a large extracellular domain, a single transmembrane helix, and a smaller cytoplasmic domain. The extracellular domain contains four distinct protein modules: 5 low density lipoprotein type A, 52 epidermal growth factor, 1 von Willebrand factor A, and 2 sea urchin-enterokinase-agrin modules. MUA-3 localizes to the hypodermal hemidesmosomes and to other sites of mechanically robust transepithelial attachments, including the rectum, vulva, mechanosensory neurons, and excretory duct\/pore. In addition, it is shown that MUA-3 colocalizes with cytoplasmic intermediate filaments (IFs) at these sites. Thus, MUA-3 appears to be a protein that links the IF cytoskeleton of nematode epithelia to the cuticle at sites of mechanical stress.<\/jats:p>","DOI":"10.1083\/jcb.200103035","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T16:46:23Z","timestamp":1027701983000},"page":"415-426","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":60,"title":["<i>mua-3<\/i>, a gene required for mechanical tissue integrity in <i>Caenorhabditis elegans,<\/i> encodes a novel transmembrane protein of epithelial attachment complexes"],"prefix":"10.1083","volume":"154","author":[{"given":"Mark","family":"Bercher","sequence":"first","affiliation":[{"name":"1Department of Biology, University of Toledo, Toledo, OH 43606"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jim","family":"Wahl","sequence":"additional","affiliation":[{"name":"1Department of Biology, University of Toledo, Toledo, OH 43606"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bruce E.","family":"Vogel","sequence":"additional","affiliation":[{"name":"2Department of Biology, Johns Hopkins University, Baltimore, MD 21218"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Charles","family":"Lu","sequence":"additional","affiliation":[{"name":"2Department of Biology, Johns Hopkins University, Baltimore, MD 21218"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Edward M.","family":"Hedgecock","sequence":"additional","affiliation":[{"name":"2Department of Biology, Johns Hopkins University, Baltimore, MD 21218"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David H.","family":"Hall","sequence":"additional","affiliation":[{"name":"3Center for Caenorhabditis elegans Anatomy, Department of Neuroscience, Albert Einstein College of Medicine, New York, NY 10461"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John D.","family":"Plenefisch","sequence":"additional","affiliation":[{"name":"1Department of Biology, University of Toledo, Toledo, OH 43606"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"291","published-online":{"date-parts":[[2001,7,23]]},"reference":[{"key":"2023072904305841100_BIB1","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1083\/jcb.114.4.715","volume":"114","year":"1991","journal-title":"J. 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