title: Rho1 regulates adherens junction remodeling by promoting recycling endosome formation through activation of myosin II.
abstract: Once adherens junctions (AJs) are formed between polarized epithelial cells they must be maintained because AJs are constantly remodeled in dynamic epithelia. AJ maintenance involves endocytosis and subsequent recycling of E-cadherin to a precise location along the basolateral membrane. In the Drosophila pupal eye epithelium, Rho1 GTPase regulates AJ remodeling through Drosophila E-cadherin (DE-cadherin) endocytosis by limiting Cdc42/Par6/aPKC complex activity. We demonstrate that Rho1 also influences AJ remodeling by regulating the formation of DE-cadherin-containing, Rab11-positive recycling endosomes in Drosophila postmitotic pupal eye epithelia. This effect of Rho1 is mediated through Rok-dependent, but not MLCK-dependent, stimulation of myosin II activity yet independent of its effects upon actin remodeling. Both Rho1 and pMLC localize on endosomal vesicles, suggesting that Rho1 might regulate the formation of recycling endosomes through localized myosin II activation. This work identifies spatially distinct functions for Rho1 in the regulation of DE-cadherin-containing vesicular trafficking during AJ remodeling in live epithelia.
authors: ICCE Institute, Washington University School of Medicine, St. Louis, MO 63110 Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110 Department of Developmental Biology, Washington University School of Medicine, St. Louis, MO 63110.
authors: Hanako
authors: H
authors: Yashiro
authors: ICCE Institute, Washington University School of Medicine, St. Louis, MO 63110 Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110.
authors: Andrew J
authors: AJ
authors: Loza
authors: Department of Genetics, Washington University School of Medicine, St. Louis, MO 63110.
authors: James B
authors: JB
authors: Skeath
authors: ICCE Institute, Washington University School of Medicine, St. Louis, MO 63110 Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110 Department of Medicine, Washington University School of Medicine, St. Louis, MO 63110 BRIGHT Institute, Washington University School of Medicine, St. Louis, MO 63110 glongmor@dom.wustl.edu.
authors: Gregory D
authors: GD
authors: Longmore
mesh_terms: D022005:Adherens Junctions / Q000378:metabolism*; D000818:Animals; D015820:Cadherins / Q000378:metabolism*; D004330:Drosophila; D029721:Drosophila Proteins / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism*; D004705:Endocytosis; D011992:Endosomes / Q000378:metabolism; D004848:Epithelium / Q000378:metabolism; D005123:Eye / Q000378:metabolism*; D019204:GTP-Binding Proteins / Q000378:metabolism; D024462:Myosin Type II / Q000378:metabolism; D010455:Peptides; D011493:Protein Kinase C / Q000378:metabolism; D021381:Protein Transport; D011679:Pupa / Q000378:metabolism; D020691:rab GTP-Binding Proteins / Q000096:biosynthesis / Q000378:metabolism*; D020741:rho GTP-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D054460:rho-Associated Kinases; D000099193:rab11 GTP-Binding Proteins
chemical_list: D015820:Cadherins; D029721:Drosophila Proteins; D019204:GTP-Binding Proteins; D024462:Myosin Type II; D010455:Peptides; D011493:Protein Kinase C; D020691:rab GTP-Binding Proteins; D020741:rho GTP-Binding Proteins; D054460:rho-Associated Kinases; C090145:Cdc42 protein, Drosophila; C501889:shg protein, Drosophila; C065738:MLCK peptide; C115015:PKC-3 protein; C559123:Rab11 protein, Drosophila; D000099193:rab11 GTP-Binding Proteins; C511153:Rho1 protein, Drosophila