{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T20:42:45Z","timestamp":1792096965798,"version":"4.4.0"},"reference-count":55,"publisher":"American Society for Microbiology","issue":"4","license":[{"start":{"date-parts":[[2012,4,1]],"date-time":"2012-04-01T00:00:00Z","timestamp":1333238400000},"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":["Eukaryot Cell"],"published-print":{"date-parts":[[2012,4]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Human Wiskott-Aldrich syndrome protein (WASP) is a scaffold linking upstream signals to the actin cytoskeleton. In response to intersectin ITSN1 and Rho GTPase Cdc42, WASP activates the Arp2\/3 complex to promote actin polymerization. The human pathogen\n                    <jats:named-content content-type=\"genus-species\">Cryptococcus neoformans<\/jats:named-content>\n                    contains the ITSN1 homolog Cin1 and the WASP homolog Wsp1, which share more homology with human proteins than those of other fungi. Here we demonstrate that Cin1, Cdc42\/Rac1, and Wsp1 function in an effector pathway similar to that of mammalian models. In the\n                    <jats:italic>cin1<\/jats:italic>\n                    mutant, expression of the autoactivated Wsp1-B-GBD allele partially suppressed the mutant defect in endocytosis, and expression of the constitutively active\n                    <jats:italic>CDC42<\/jats:italic>\n                    <jats:sup>\n                      <jats:italic>Q61L<\/jats:italic>\n                    <\/jats:sup>\n                    allele restored normal actin cytoskeleton structures. Similar phenotypic suppression can be obtained by the expression of a Cdc42-green fluorescent protein (GFP)-Wsp1 fusion protein. In addition, Rac1, which was found to exhibit a role in early endocytosis, activates Wsp1 to regulate vacuole fusion. Rac1 interacted with Wsp1 and depended on Wsp1 for its vacuolar membrane localization. Expression of the Wsp1-B-GBD allele restored vacuolar membrane fusion in the\n                    <jats:italic>rac1<\/jats:italic>\n                    mutant. Collectively, our studies suggest novel ways in which this pathogenic fungus has adapted conserved signaling pathways to control vesicle transport and actin organization, likely benefiting survival within infected hosts.\n                  <\/jats:p>","DOI":"10.1128\/ec.00011-12","type":"journal-article","created":{"date-parts":[[2012,2,11]],"date-time":"2012-02-11T00:16:53Z","timestamp":1328919413000},"page":"471-481","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":19,"title":["Wsp1 Is Downstream of Cin1 and Regulates Vesicle Transport and Actin Cytoskeleton as an Effector of Cdc42 and Rac1 in Cryptococcus neoformans"],"prefix":"10.1128","volume":"11","author":[{"given":"Gui","family":"Shen","sequence":"first","affiliation":[{"name":"The Research Institute for Children, New Orleans, Louisiana, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erxun","family":"Zhou","sequence":"additional","affiliation":[{"name":"The Research Institute for Children, New Orleans, Louisiana, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J. Andrew","family":"Alspaugh","sequence":"additional","affiliation":[{"name":"Departments of Medicine, Duke University School of Medicine, Durham, North Carolina, USA"},{"name":"Molecular Genetics and Microbiology, Duke University School of Medicine, Durham, North Carolina, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ping","family":"Wang","sequence":"additional","affiliation":[{"name":"The Research Institute for Children, New Orleans, Louisiana, USA"},{"name":"Departments of Microbiology, Immunology, and Parasitology, New Orleans, Louisiana, USA"},{"name":"Pediatrics, Louisiana State University Health Sciences Center, New Orleans, Louisiana, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1242\/jcs.110.6.707"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0960-9822(02)00423-2"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2009.07019.x"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/EC.5.2.321-329.2006"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1091\/mbc.5.9.1023"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1242\/jcs.00319"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.3201\/eid0401.980109"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2011.07632.x"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature09623"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1186\/gb-2002-3-2-reviews0002"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1099\/00221287-148-8-2607"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1007\/978-0-387-93877-6_15"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1038\/35083087"},{"key":"e_1_3_3_15_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pbio.0060001"},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrm2026"},{"key":"e_1_3_3_17_2","doi-asserted-by":"publisher","DOI":"10.1038\/371168a0"},{"key":"e_1_3_3_18_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2010.07525.x"},{"key":"e_1_3_3_19_2","unstructured":"HeitmanJ\nKozelTR\nKwon-ChungKJ\nPerfectJR\nCasadevallA. 2011. 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