scholarly journals Sequential Roles of Cdc42, Par-6, aPKC, and Lgl in the Establishment of Epithelial Polarity during Drosophila Embryogenesis

2004 ◽  
Vol 6 (6) ◽  
pp. 845-854 ◽  
Author(s):  
Andrea Hutterer ◽  
Joerg Betschinger ◽  
Mark Petronczki ◽  
Juergen A Knoblich
Keyword(s):  
Epithelial Polarity ◽  
Drosophila Embryogenesis

scholarly journals Drosophilachemmutations disrupt epithelial polarity in Drosophila embryos

PeerJ ◽  
2016 ◽  
Vol 4 ◽  
pp. e2731
Author(s):  
José M. Zamudio-Arroyo ◽  
Juan R. Riesgo-Escovar
Keyword(s):  
Similar Pattern ◽  
Gene Discovery ◽  
Dorsal Closure ◽  
Epithelial Polarity ◽  
Developmental Gene ◽  
Drosophila Embryogenesis ◽  
Powerful System ◽  
Maternal Contribution ◽  
New Alleles ◽  
Drosophila Embryos

Drosophila embryogenesis has proven to be an extremely powerful system for developmental gene discovery and characterization. We isolated five new EMS-induced alleles that do not complement thel(3R)5G83lethal line isolated in the Nüsslein-Volhard and Wieschaus screens. We have named this locuschem. Lethality of the new alleles as homozygous zygotic mutants is not completely penetrant, and they have an extended phenocritical period. Like the original allele, a fraction of mutant embryos die with cuticular defects, notably head involution and dorsal closure defects. Embryonic defects are much more extreme in germline clones, where the majority of mutant embryos die during embryogenesis and do not form cuticle, implying a strongchemmaternal contribution.chemmutations genetically interact with mutations in cytoskeletal genes (arm) and with mutations in the epithelial polarity genescoracle, crumbs,andyurt.chemmutants dorsal open defects are similar to those present inyurtmutants, and, likewise, they have epithelial polarity defects.chem1andchem3mutations suppressyurt3, andchem3mutants suppresscrumbs1mutations. In contrast,chem1andcoracle2mutations enhance each other. Compared to controls, inchemmutants in embryonic lateral epithelia Crumbs expression is mislocalized and reduced, Coracle is increased and mislocalized basally at embryonic stages 13–14, then reduced at stage 16. Arm expression has a similar pattern but levels are reduced.

scholarly journals Interaction of phosphorylated Rab11-FIP2 with Eps15 regulates apical junction composition

2017 ◽  
Vol 28 (8) ◽  
pp. 1088-1100 ◽  
Author(s):  
Lynne A. Lapierre ◽  
Elizabeth H. Manning ◽  
Kenya M. Mitchell ◽  
Cathy M. Caldwell ◽  
James R. Goldenring
Keyword(s):  
Mdck Cells ◽  
Three Dimensional ◽  
3D Culture ◽  
Cyst Formation ◽  
Epithelial Polarity ◽  
Lateral Membrane ◽  
Low Calcium ◽  
Single Lumen ◽  
Apical Junctions ◽  
Temporal Localization

MARK2 regulates the establishment of polarity in Madin–Darby canine kidney (MDCK) cells in part through phosphorylation of serine 227 of Rab11-FIP2. We identified Eps15 as an interacting partner of phospho-S227-Rab11-FIP2 (pS227-FIP2). During recovery from low calcium, Eps15 localized to the lateral membrane before pS227-FIP2 arrival. Later in recovery, Eps15 and pS227-FIP2 colocalized at the lateral membrane. In MDCK cells expressing the pseudophosphorylated FIP2 mutant FIP2(S227E), during recovery from low calcium, Eps15 was trapped and never localized to the lateral membrane. Mutation of any of the three NPF domains within GFP-FIP2(S227E) rescued Eps15 localization at the lateral membrane and reestablished single-lumen cyst formation in GFP-FIP2(S227E)–expressing cells in three-dimensional (3D) culture. Whereas expression of GFP-FIP2(S227E) induced the loss of E-cadherin and occludin, mutation of any of the NPF domains of GFP-FIP2(S227E) reestablished both proteins at the apical junctions. Knockdown of Eps15 altered the spatial and temporal localization of pS227-FIP2 and also elicited formation of multiple lumens in MDCK 3D cysts. Thus an interaction of Eps15 and pS227-FIP2 at the appropriate time and location in polarizing cells is necessary for proper establishment of epithelial polarity.

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