{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T19:27:31Z","timestamp":1792697251384,"version":"4.5.0"},"reference-count":68,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2020,4,23]],"date-time":"2020-04-23T00:00:00Z","timestamp":1587600000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01DK096586"],"award-info":[{"award-number":["R01DK096586"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["K08DK115901"],"award-info":[{"award-number":["K08DK115901"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R25DK101398"],"award-info":[{"award-number":["R25DK101398"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["1S10RR031563-01"],"award-info":[{"award-number":["1S10RR031563-01"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["1S10OD021577-01"],"award-info":[{"award-number":["1S10OD021577-01"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["P30DK043351"],"award-info":[{"award-number":["P30DK043351"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100012489","name":"Boston Area Diabetes Endocrinology Research Center","doi-asserted-by":"publisher","award":["P30DK057521"],"award-info":[{"award-number":["P30DK057521"]}],"id":[{"id":"10.13039\/100012489","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>We previously showed that in polarized Madin\u2013Darby canine kidney (MDCK) cells, aquaporin-2 (AQP2) is continuously targeted to the basolateral plasma membrane from which it is rapidly retrieved by clathrin-mediated endocytosis. It then undertakes microtubule-dependent transcytosis toward the apical plasma membrane. In this study, we found that treatment with chlorpromazine (CPZ, an inhibitor of clathrin-mediated endocytosis) results in AQP2 accumulation in the basolateral, but not the apical plasma membrane of epithelial cells. In MDCK cells, both AQP2 and clathrin were concentrated in the basolateral plasma membrane after CPZ treatment (100 \u00b5M for 15 min), and endocytosis was reduced. Then, using rhodamine phalloidin staining, we found that basolateral, but not apical, F-actin was selectively reduced by CPZ treatment. After incubation of rat kidney slices in situ with CPZ (200 \u00b5M for 15 min), basolateral AQP2 and clathrin were increased in principal cells, which simultaneously showed a significant decrease of basolateral compared to apical F-actin staining. These results indicate that clathrin-dependent transcytosis of AQP2 is an essential part of its trafficking pathway in renal epithelial cells and that this process can be inhibited by selectively depolymerizing the basolateral actin pool using CPZ.<\/jats:p>","DOI":"10.3390\/cells9041057","type":"journal-article","created":{"date-parts":[[2020,4,23]],"date-time":"2020-04-23T10:46:22Z","timestamp":1587638782000},"page":"1057","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":32,"title":["Chlorpromazine Induces Basolateral Aquaporin-2 Accumulation via F-Actin Depolymerization and Blockade of Endocytosis in Renal Epithelial Cells"],"prefix":"10.3390","volume":"9","author":[{"given":"Richard","family":"Bouley","sequence":"first","affiliation":[{"name":"Program in Membrane Biology and Nephrology Division, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02114 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4262-4386","authenticated-orcid":false,"given":"Naofumi","family":"Yui","sequence":"additional","affiliation":[{"name":"Program in Membrane Biology and Nephrology Division, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02114 USA"},{"name":"Department of Nephrology, Tokyo Medical and Dental University, Tokyo 113-8519, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Abby","family":"Terlouw","sequence":"additional","affiliation":[{"name":"Program in Membrane Biology and Nephrology Division, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02114 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6615-3761","authenticated-orcid":false,"given":"Pui W.","family":"Cheung","sequence":"additional","affiliation":[{"name":"Program in Membrane Biology and Nephrology Division, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02114 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5011-7798","authenticated-orcid":false,"given":"Dennis","family":"Brown","sequence":"additional","affiliation":[{"name":"Program in Membrane Biology and Nephrology Division, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02114 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,4,23]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1146\/annurev-pharmtox-010919-023654","article-title":"Targeting the Trafficking of Kidney Water Channels for Therapeutic Benefit","volume":"60","author":"Cheung","year":"2020","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1038\/361549a0","article-title":"Cloning and expression of apical membrane water channel of rat kidney collecting tubule","volume":"361","author":"Fushimi","year":"1993","journal-title":"Nat."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1073\/pnas.92.4.1013","article-title":"Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane","volume":"92","author":"Nielsen","year":"1995","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_4","first-page":"95","article-title":"The Trafficking of the Water Channel Aquaporin-2 in Renal Principal Cells\u2014a Potential Target for Pharmacological Intervention in Cardiovascular Diseases","volume":"7","author":"Schulz","year":"2016","journal-title":"Front. Pharmacol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1097\/MNH.0b013e3283094eb1","article-title":"Phosphorylation events and the modulation of aquaporin 2 cell surface expression","volume":"17","author":"Brown","year":"2008","journal-title":"Curr. Opin. Nephrol. Hypertens."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"7159","DOI":"10.1073\/pnas.0600895103","article-title":"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: Regulation of aquaporin-2 phosphorylation at two sites","volume":"103","author":"Hoffert","year":"2006","journal-title":"Proc. Natl. Acad. Sci."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"24617","DOI":"10.1074\/jbc.M803074200","article-title":"Vasopressin-stimulated increase in phosphorylation at Ser269 potentiates plasma membrane retention of aquaporin-2","volume":"283","author":"Hoffert","year":"2008","journal-title":"J. Boil. Chem."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1038\/ki.2008.505","article-title":"Serine 269 phosphorylated aquaporin-2 is targeted to the apical membrane of collecting duct principal cells","volume":"75","author":"Moeller","year":"2008","journal-title":"Kidney Int."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"F691","DOI":"10.1152\/ajprenal.00284.2006","article-title":"Dynamics of aquaporin-2 serine-261 phosphorylation in response to short-term vasopressin treatment in collecting duct","volume":"292","author":"Hoffert","year":"2007","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"F673","DOI":"10.1152\/ajprenal.00152.2015","article-title":"Characterization of the putative phosphorylation sites of the AQP2 C terminus and their role in AQP2 trafficking in LLC-PK1 cells","volume":"309","author":"Arthur","year":"2015","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"F233","DOI":"10.1152\/ajprenal.00179.2003","article-title":"Inhibition of endocytosis causes phosphorylation (S256)-independent plasma membrane accumulation of AQP2","volume":"286","author":"Lu","year":"2004","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"F246","DOI":"10.1152\/ajprenal.00437.2005","article-title":"Methyl-\u03b2-cyclodextrin induces vasopressin-independent apical accumulation of aquaporin-2 in the isolated, perfused rat kidney","volume":"291","author":"Russo","year":"2006","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1042\/BC20040054","article-title":"Aquaporin 2 (AQP2) and vasopressin type 2 receptor (V2R) endocytosis in kidney epithelial cells: AQP2 is located in \u2018endocytosis-resistant\u2019 membrane domains after vasopressin treatment","volume":"98","author":"Bouley","year":"2006","journal-title":"Boil. Cell"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"F309","DOI":"10.1152\/ajprenal.00001.2011","article-title":"Simvastatin enhances aquaporin-2 surface expression and urinary concentration in vasopressin-deficient Brattleboro rats through modulation of Rho GTPase","volume":"301","author":"Li","year":"2011","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"C1476","DOI":"10.1152\/ajpcell.00344.2008","article-title":"A fluorimetry-based ssYFP secretion assay to monitor vasopressin-induced exocytosis in LLC-PK1 cells expressing aquaporin-2","volume":"295","author":"Hasler","year":"2008","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"F214","DOI":"10.1152\/ajprenal.1993.265.2.F214","article-title":"Kinetic model of water and urea permeability regulation by vasopressin in collecting duct","volume":"265","author":"Knepper","year":"1993","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"28721","DOI":"10.1074\/jbc.M611101200","article-title":"Heat Shock Protein 70 Interacts with Aquaporin-2 and Regulates Its Trafficking*","volume":"282","author":"Lu","year":"2007","journal-title":"J. Boil. Chem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1007\/s00424-012-1129-4","article-title":"Cell biology of vasopressin-regulated aquaporin-2 trafficking","volume":"464","author":"Moeller","year":"2012","journal-title":"Pfl\u00fcgers Archiv - Eur. J. Physiol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1073\/pnas.0910683107","article-title":"Phosphorylation of aquaporin-2 regulates its endocytosis and protein\u2013protein interactions","volume":"107","author":"Moeller","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1083\/jcb.200709177","article-title":"Reciprocal interaction with G-actin and tropomyosin is essential for aquaporin-2 trafficking","volume":"182","author":"Noda","year":"2008","journal-title":"J. Cell Boil."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1242\/bio.2011042","article-title":"AQP2 is necessary for vasopressin- and forskolin-mediated filamentous actin depolymerization in renal epithelial cells","volume":"1","author":"Yui","year":"2011","journal-title":"Boil. Open"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"F893","DOI":"10.1152\/ajprenal.00387.2002","article-title":"The ins and outs of aquaporin-2 trafficking","volume":"284","author":"Brown","year":"2003","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"F874","DOI":"10.1152\/ajprenal.2000.279.5.F874","article-title":"Expression of aquaporins in the renal connecting tubule","volume":"279","author":"Coleman","year":"2000","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"F87","DOI":"10.1152\/ajprenal.00431.2006","article-title":"Long-term aldosterone treatment induces decreased apical but increased basolateral expression of AQP2 in CCD of rat kidney","volume":"293","author":"Nielsen","year":"2007","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_25","first-page":"e36","article-title":"Oxytocin induces apical and basolateral redistribution of aquaporin-2 in rat kidney","volume":"93","author":"Jeon","year":"2003","journal-title":"Nephron"},{"key":"ref_26","first-page":"1101","article-title":"Hypertonicity Is Involved in Redirecting the Aquaporin-2 Water Channel into the Basolateral, Instead of the Apical, Plasma Membrane of Renal Epithelial Cells","volume":"278","author":"Breton","year":"2002","journal-title":"J. Boil. Chem."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1016\/S0092-8674(00)81435-X","article-title":"Sec6\/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells","volume":"93","author":"Grindstaff","year":"1998","journal-title":"Cell"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1095","DOI":"10.1074\/mcp.M500049-MCP200","article-title":"Large-Scale Protein Identification in Intracellular Aquaporin-2 Vesicles from Renal Inner Medullary Collecting Duct","volume":"4","author":"Barile","year":"2005","journal-title":"Mol. Cell. Proteom."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1506","DOI":"10.1681\/ASN.2012010079","article-title":"Aquaporin 2 Promotes Cell Migration and Epithelial Morphogenesis","volume":"23","author":"Chen","year":"2012","journal-title":"J. Am. Soc. Nephrol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"C38","DOI":"10.1152\/ajpcell.00109.2012","article-title":"Basolateral targeting and microtubule-dependent transcytosis of the aquaporin-2 water channel","volume":"304","author":"Yui","year":"2012","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"17119","DOI":"10.1073\/pnas.1309219110","article-title":"Quantitative apical membrane proteomics reveals vasopressin-induced actin dynamics in collecting duct cells","volume":"110","author":"Loo","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"C33","DOI":"10.1152\/ajpcell.00348.2012","article-title":"Caring about the other 47% of the water channels. Focus on \"Basolateral targeting and microtubule-dependent transcytosis of the aquaporin-2 water channel\"","volume":"304","author":"Okamoto","year":"2012","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"C85","DOI":"10.1152\/ajpcell.00118.2009","article-title":"Phorbol 12-myristate 13-acetate-induced endocytosis of the Na-K-2Cl cotransporter in MDCK cells is associated with a clathrin-dependent pathway","volume":"298","author":"Mykoniatis","year":"2009","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"C1389","DOI":"10.1152\/ajpcell.00098.2009","article-title":"FAPP2 is required for aquaporin-2 apical sorting at trans-Golgi network in polarized MDCK cells","volume":"297","author":"Yui","year":"2009","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1493","DOI":"10.1681\/ASN.V8101493","article-title":"Aquaporin-2 transfection of Madin-Darby canine kidney cells reconstitutes vasopressin-regulated transcellular osmotic water transport","volume":"8","author":"Deen","year":"1997","journal-title":"J. Am. Soc. Nephrol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"3105","DOI":"10.1681\/ASN.2015080903","article-title":"EGF Receptor Inhibition by Erlotinib Increases Aquaporin 2\u2013Mediated Renal Water Reabsorption","volume":"27","author":"Cheung","year":"2016","journal-title":"J. Am. Soc. Nephrol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1172\/JCI9594","article-title":"Nitric oxide and atrial natriuretic factor stimulate cGMP-dependent membrane insertion of aquaporin 2 in renal epithelial cells","volume":"106","author":"Bouley","year":"2000","journal-title":"J. Clin. Investig."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1681\/ASN.2009121267","article-title":"Calcitonin has a vasopressin-like effect on aquaporin-2 trafficking and urinary concentration","volume":"22","author":"Bouley","year":"2010","journal-title":"J. Am. Soc. Nephrol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1016\/j.bbamem.2013.06.004","article-title":"Actin directly interacts with different membrane channel proteins and influences channel activities: AQP2 as a model","volume":"1838","author":"Sasaki","year":"2014","journal-title":"Biochim. Biophys. Acta (BBA) - Biomembr."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"4375","DOI":"10.1210\/en.2004-0073","article-title":"Aquaporin-2 Is Retrieved to the Apical Storage Compartment via Early Endosomes and Phosphatidylinositol 3-Kinase-Dependent Pathway","volume":"145","author":"Tajika","year":"2004","journal-title":"Endocrinology"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"C757","DOI":"10.1152\/ajpcell.1993.265.3.C757","article-title":"Vasopressin depolymerizes apical F-actin in rat inner medullary collecting duct","volume":"265","author":"Simon","year":"1993","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1631","DOI":"10.1021\/jm00392a019","article-title":"Charged analogues of chlorpromazine as dopamine antagonists","volume":"30","author":"Harrold","year":"1987","journal-title":"J. Med. Chem."},{"key":"ref_43","first-page":"171","article-title":"Differential inhibition of calmodulin-sensitive phosphodiesterase and Ca++-adenosine triphosphatase by chlorpromazine-linked calmodulin","volume":"243","author":"Prozialeck","year":"1987","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_44","first-page":"2100","article-title":"Dynamin- and Clathrin-Dependent Endocytosis in African Swine Fever Virus Entry","volume":"84","author":"Alonso","year":"2009","journal-title":"J. Virol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"1535","DOI":"10.1099\/0022-1317-83-7-1535","article-title":"Dissecting virus entry via endocytosis","volume":"83","author":"Sieczkarski","year":"2002","journal-title":"J. Gen. Virol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1083\/jcb.123.5.1107","article-title":"Mis-assembly of clathrin lattices on endosomes reveals a regulatory switch for coated pit formation","volume":"123","author":"Wang","year":"1993","journal-title":"J. Cell Boil."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1006\/abbi.1999.1260","article-title":"Effects of Chlorpromazine on Actin Polymerization: Slackening of Filament Elongation and Filament Annealing","volume":"369","author":"Milzani","year":"1999","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1007\/BF00852577","article-title":"The effect of vasopressin on the cytoskeleton of the epithelial cell","volume":"7","author":"Hays","year":"1993","journal-title":"Pediatr. Nephrol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"2881","DOI":"10.1681\/ASN.2005020190","article-title":"Bradykinin Signaling Counteracts cAMP-Elicited Aquaporin 2 Translocation in Renal Cells","volume":"16","author":"Tamma","year":"2005","journal-title":"J. Am. Soc. Nephrol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"F1092","DOI":"10.1152\/ajprenal.0091.2001","article-title":"Rho inhibits cAMP-induced translocation of aquaporin-2 into the apical membrane of renal cells","volume":"281","author":"Tamma","year":"2001","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1519","DOI":"10.1242\/jcs.00355","article-title":"cAMP-induced AQP2 translocation is associated with RhoA inhibition through RhoA phosphorylation and interaction with RhoGDI","volume":"116","author":"Tamma","year":"2003","journal-title":"J. Cell Sci."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"3285","DOI":"10.1242\/jcs.00640","article-title":"The prostaglandin E2 analogue sulprostone antagonizes vasopressin-induced antidiuresis through activation of Rho","volume":"116","author":"Tamma","year":"2003","journal-title":"J. Cell Sci."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1242\/jcs.113.11.1985","article-title":"The phosphatase inhibitor okadaic acid induces AQP2 translocation independently from AQP2 phosphorylation in renal collecting duct cells","volume":"113","author":"Valenti","year":"2000","journal-title":"J. Cell Sci."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"1341","DOI":"10.1016\/j.bbamcr.2018.06.013","article-title":"Dynamic L-type CaV1.2 channel trafficking facilitates CaV1.2 clustering and cooperative gating","volume":"1865","author":"Ghosh","year":"2018","journal-title":"Biochim. Biophys. Acta (BBA) - Bioenerg."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"42300","DOI":"10.1074\/jbc.M510920200","article-title":"Disruption of Microtubules Ablates the Specificity of Insulin Signaling to GLUT4 Translocation in 3T3-L1 Adipocytes","volume":"280","author":"Huang","year":"2005","journal-title":"J. Boil. Chem."},{"key":"ref_56","doi-asserted-by":"crossref","unstructured":"Karpushev, A.V., Ilatovskaya, D.V., Pavlov, T.S., Negulyaev, Y.A., and Staruschenko, A. (2010). Intact Cytoskeleton Is Required for Small G Protein Dependent Activation of the Epithelial Na+ Channel. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0008827"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"674","DOI":"10.1016\/j.bbamem.2013.08.026","article-title":"Tubulin, actin and heterotrimeric G proteins: Coordination of signaling and structure","volume":"1838","author":"Schappi","year":"2013","journal-title":"Biochim. Biophys. Acta (BBA) - Bioenerg."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.jcf.2009.10.002","article-title":"Entry of Burkholderia organisms into respiratory epithelium: CFTR, microfilament and microtubule dependence","volume":"9","author":"Taylor","year":"2009","journal-title":"J. Cyst. Fibros."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1083\/jcb.201402037","article-title":"Isotropic actomyosin dynamics promote organization of the apical cell cortex in epithelial cells","volume":"207","author":"Klingner","year":"2014","journal-title":"J. Cell Boil."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s00418-005-0010-3","article-title":"Differential regulation of AQP2 trafficking in endosomes by microtubules and actin filaments","volume":"124","author":"Tajika","year":"2005","journal-title":"Histochem. Cell Boil."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"7689","DOI":"10.1073\/pnas.1407351111","article-title":"Polarized deposition of basement membrane proteins depends on Phosphatidylinositol synthase and the levels of Phosphatidylinositol 4,5-bisphosphate","volume":"111","author":"Devergne","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1016\/j.bbamcr.2006.06.013","article-title":"ERM proteins in epithelial cell organization and functions","volume":"1773","author":"Louvard","year":"2007","journal-title":"Biochim. Biophys. Acta (BBA) - Bioenerg."},{"key":"ref_63","first-page":"963","article-title":"Phosphatidylinositol-3,4,5-trisphosphate regulates the formation of the basolateral plasma membrane in epithelial cells","volume":"8","author":"Yu","year":"2006","journal-title":"Nature"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1016\/j.cell.2006.11.051","article-title":"PTEN-Mediated Apical Segregation of Phosphoinositides Controls Epithelial Morphogenesis through Cdc42","volume":"128","author":"Gassama","year":"2007","journal-title":"Cell"},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"Rice, W.L., Li, W., Mamuya, F., McKee, M., Paunescu, T., and Lu, H.A.J. (2015). Polarized Trafficking of AQP2 Revealed in Three Dimensional Epithelial Culture. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0131719"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1039","DOI":"10.1016\/j.bbrc.2017.06.162","article-title":"Ser-261 phospho-regulation is involved in pS256 and pS269-mediated aquaporin-2 apical translocation","volume":"490","author":"Yui","year":"2017","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"F998","DOI":"10.1152\/ajprenal.00257.2001","article-title":"Aquaporin-2 localization in clathrin-coated pits: Inhibition of endocytosis by dominant-negative dynamin","volume":"282","author":"Sun","year":"2002","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1007\/s00424-011-1007-5","article-title":"Fluvastatin modulates renal water reabsorption in vivo through increased AQP2 availability at the apical plasma membrane of collecting duct cells","volume":"462","author":"Procino","year":"2011","journal-title":"Pfl\u00fcgers Archiv - Eur. J. 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