{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,15]],"date-time":"2026-11-15T12:07:40Z","timestamp":1794744460124,"version":"4.9.1"},"reference-count":75,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2005,12,5]],"date-time":"2005-12-05T00:00:00Z","timestamp":1133740800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The Plant Journal"],"published-print":{"date-parts":[[2006,1]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>Since copper (Cu) is essential in key physiological oxidation reactions, organisms have developed strategies for handling Cu while avoiding its potentially toxic effects. Among the tools that have evolved to cope with Cu is a network of Cu homeostasis factors such as Cu\u2010transporting P\u2010type ATPases that play a key role in transmembrane Cu transport. In this work we present the functional characterization of an Arabidopsis Cu\u2010transporting P\u2010type ATPase, denoted heavy metal ATPase 5 (HMA5), and its interaction with Arabidopsis metallochaperones. <jats:italic>HMA5<\/jats:italic> is primarily expressed in roots, and is strongly and specifically induced by Cu in whole plants. We have identified and characterized plants carrying two independent T\u2010DNA insertion alleles, <jats:italic>hma5\u20101<\/jats:italic> and <jats:italic>hma5\u20102<\/jats:italic>. Both mutants are hypersensitive to Cu but not to other metals such as iron, zinc or cadmium. Interestingly, root tips from Cu\u2010treated <jats:italic>hma5<\/jats:italic> mutants exhibit a wave\u2010like phenotype at early stages and later on main root growth completely arrests whereas lateral roots emerge near the crown. Accordingly, these lines accumulate Cu in roots to a greater extent than wild\u2010type plants under Cu excess. Finally, yeast two\u2010hybrid experiments demonstrate that the metal\u2010binding domains of HMA5 interact with Arabidopsis ATX1\u2010like Cu chaperones, and suggest a regulatory role for the plant\u2010specific domain of the CCH Cu chaperone. Based on these findings, we propose a role for HMA5 in Cu compartmentalization and detoxification.<\/jats:p>","DOI":"10.1111\/j.1365-313x.2005.02601.x","type":"journal-article","created":{"date-parts":[[2005,12,5]],"date-time":"2005-12-05T10:41:42Z","timestamp":1133779302000},"page":"225-236","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":320,"title":["The Arabidopsis heavy metal P\u2010type ATPase HMA5 interacts with metallochaperones and functions in copper detoxification of roots"],"prefix":"10.1111","volume":"45","author":[{"given":"Nuria","family":"Andr\u00e9s\u2010Col\u00e1s","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vicente","family":"Sancen\u00f3n","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Susana","family":"Rodr\u00edguez\u2010Navarro","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sonia","family":"Mayo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dennis J.","family":"Thiele","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joseph 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