{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T04:40:24Z","timestamp":1791348024692,"version":"4.3.1"},"reference-count":67,"publisher":"American Society for Microbiology","issue":"5","license":[{"start":{"date-parts":[[2013,8,27]],"date-time":"2013-08-27T00:00:00Z","timestamp":1377561600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-sa\/3.0\/"},{"start":{"date-parts":[[2013,11,1]],"date-time":"2013-11-01T00:00:00Z","timestamp":1383264000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["mBio"],"published-print":{"date-parts":[[2013,11]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Clathrin-mediated endocytosis (CME) is conserved among eukaryotes and has been extensively analyzed at a molecular level. Here, we present an analysis of CME in the human fungal pathogen\n            <jats:named-content content-type=\"genus-species\">Candida albicans<\/jats:named-content>\n            that shows the same modular structure as those in other fungi and mammalian cells. Intriguingly,\n            <jats:named-content content-type=\"genus-species\">C. albicans<\/jats:named-content>\n            is perfectly viable in the absence of Arp2\/3, an essential component of CME in other systems. In\n            <jats:named-content content-type=\"genus-species\">C. albicans<\/jats:named-content>\n            , Arp2\/3 function remains essential for CME as all 15 proteins tested that participate in CME, including clathrin, lose their characteristic dynamics observed in wild-type (WT) cells. However, since\n            <jats:italic>arp2<\/jats:italic>\n            \/\n            <jats:italic>3<\/jats:italic>\n            cells are still able to endocytose lipids and fluid-phase markers, but not the Ste2 and Mup1 plasma membrane proteins, there must be an alternate clathrin-independent pathway we term Arp2\/3-independent endocytosis (AIE). Characterization of AIE shows that endocytosis in\n            <jats:italic>arp2<\/jats:italic>\n            mutants relies on actin cables and other Arp2\/3-independent actin structures, as inhibition of actin functions prevented cargo uptake in\n            <jats:italic>arp2<\/jats:italic>\n            \/\n            <jats:italic>3<\/jats:italic>\n            mutants. Transmission electron microscopy (TEM) showed that\n            <jats:italic>arp2<\/jats:italic>\n            \/\n            <jats:italic>3<\/jats:italic>\n            mutants still formed invaginating tubules, cell structures whose proper functions are believed to heavily rely on Arp2\/3. Finally, Prk1 and Sjl2, two proteins involved in patch disassembly during CME, were not correctly localized to sites of endocytosis in\n            <jats:italic>arp2<\/jats:italic>\n            mutants, implying a role of Arp2\/3 in CME patch disassembly. Overall,\n            <jats:named-content content-type=\"genus-species\">C. albicans<\/jats:named-content>\n            contains an alternative endocytic pathway (AIE) that relies on actin cable function to permit clathrin-independent endocytosis (CIE) and provides a system to further explore alternate endocytic routes that likely exist in fungal species.\n          <\/jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE<\/jats:bold>\n            There is a well-established process of endocytosis that is generally used by eukaryotic cells termed clathrin-mediated endocytosis (CME). Although the details are somewhat different between lower and higher eukaryotes, CME appears to be the dominant endocytic process in all eukaryotes. While fungi such as\n            <jats:named-content content-type=\"genus-species\">Saccharomyces cerevisiae<\/jats:named-content>\n            have proven excellent models for dissecting the molecular details of endocytosis, loss of CME is so detrimental that it has been difficult to study alternate pathways functioning in its absence. Although the fungal pathogen\n            <jats:named-content content-type=\"genus-species\">Candida albicans<\/jats:named-content>\n            has a CME pathway that functions similarly to that of\n            <jats:named-content content-type=\"genus-species\">S. cerevisiae<\/jats:named-content>\n            , inactivation of this pathway does not compromise growth of yeast-form\n            <jats:named-content content-type=\"genus-species\">C. albicans<\/jats:named-content>\n            . In these cells, lipids and fluid-phase molecules are still endocytosed in an actin-dependent manner, but membrane proteins are not. Thus,\n            <jats:named-content content-type=\"genus-species\">C. albicans<\/jats:named-content>\n            provides a powerful model for the analysis of CME-independent endocytosis in lower eukaryotes.\n          <\/jats:p>","DOI":"10.1128\/mbio.00476-13","type":"journal-article","created":{"date-parts":[[2013,8,28]],"date-time":"2013-08-28T02:02:03Z","timestamp":1377655323000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":45,"title":["Clathrin- and Arp2\/3-Independent Endocytosis in the Fungal Pathogen Candida albicans"],"prefix":"10.1128","volume":"4","author":[{"given":"Elias","family":"Epp","sequence":"first","affiliation":[{"name":"Department of Biology, McGill University, Montreal, Quebec, Canada"},{"name":"Genetics Group, Biotechnology Research Institute, National Research Council of Canada, Montreal, Quebec, 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