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Although its exact role is unknown, the head domain likely mediates developmental and cancer-associated events linked to p120-1A expression (e.g., motility, invasion, metastasis). Here we identified delta-interacting protein A (DIPA) as the first head domain\u2013specific binding partner and candidate mediator of isoform 1A activity. DIPA colocalizes with AJs in a p120-1A- but not 3A-dependent manner. Moreover, all DIPA family members (Ccdc85a, Ccdc85b\/DIPA, and Ccdc85c) interact reciprocally with p120 family members (p120, \u03b4-catenin, p0071, and ARVCF), suggesting significant functional overlap. During zebrafish neural tube development, both knockdown and overexpression of DIPA phenocopy N-cadherin mutations, an effect bearing functional ties to a reported mouse hydrocephalus phenotype associated with Ccdc85c. These studies identify a novel, highly conserved interaction between two protein families that may participate either individually or collectively in N-cadherin\u2013mediated development.<\/jats:p>","DOI":"10.1091\/mbc.e13-08-0492","type":"journal-article","created":{"date-parts":[[2014,7,10]],"date-time":"2014-07-10T03:53:26Z","timestamp":1404964406000},"page":"2592-2603","source":"Crossref","is-referenced-by-count":33,"title":["DIPA-family coiled-coils bind conserved isoform-specific head domain of p120-catenin family: potential roles in hydrocephalus and heterotopia"],"prefix":"10.1091","volume":"25","author":[{"given":"Nicholas O.","family":"Markham","sequence":"first","affiliation":[{"name":"Vanderbilt-Ingram Cancer Center, Cancer Biology Department, Vanderbilt University Medical Center, Nashville, TN 37232"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Caleb A.","family":"Doll","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, 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