Faculty Opinions recommendation of Amnioserosa cell constriction but not epidermal actin cable tension autonomously drives dorsal closure.

Author(s):  
Ronen Zaidel-Bar
2016 ◽  
Vol 18 (11) ◽  
pp. 1161-1172 ◽  
Author(s):  
Laurynas Pasakarnis ◽  
Erich Frei ◽  
Emmanuel Caussinus ◽  
Markus Affolter ◽  
Damian Brunner

2002 ◽  
Vol 12 (14) ◽  
pp. 1245-1250 ◽  
Author(s):  
Antonio Jacinto ◽  
William Wood ◽  
Sarah Woolner ◽  
Charlotte Hiley ◽  
Laura Turner ◽  
...  

2011 ◽  
Vol 22 (12) ◽  
pp. 2010-2030 ◽  
Author(s):  
Wangsun Choi ◽  
Kuo-Chen Jung ◽  
Kevin S. Nelson ◽  
Manzoor A. Bhat ◽  
Greg J. Beitel ◽  
...  

Adherens and tight junctions play key roles in assembling epithelia and maintaining barriers. In cell culture zonula occludens (ZO)–family proteins are important for assembly/maturation of both tight and adherens junctions (AJs). Genetic studies suggest that ZO proteins are important during normal development, but interpretation of mouse and fly studies is limited by genetic redundancy and/or a lack of null alleles. We generated null alleles of the single Drosophila ZO protein Polychaetoid (Pyd). Most embryos lacking Pyd die with striking defects in morphogenesis of embryonic epithelia including the epidermis, segmental grooves, and tracheal system. Pyd loss does not dramatically affect AJ protein localization or initial localization of actin and myosin during dorsal closure. However, Pyd loss does affect several cell behaviors that drive dorsal closure. The defects, which include segmental grooves that fail to retract, a disrupted leading edge actin cable, and reduced zippering as leading edges meet, closely resemble defects in canoe zygotic null mutants and in embryos lacking the actin regulator Enabled (Ena), suggesting that these proteins act together. Canoe (Cno) and Pyd are required for proper Ena localization during dorsal closure, and strong genetic interactions suggest that Cno, Pyd, and Ena act together in regulating or anchoring the actin cytoskeleton during dorsal closure.


2001 ◽  
Vol 84 (3) ◽  
pp. 39-46
Author(s):  
Hitoshi Furuta ◽  
Masakatsu Kaneyoshi ◽  
Hiroshi Tanaka ◽  
Eiichi Watanabe

Genetics ◽  
2003 ◽  
Vol 165 (1) ◽  
pp. 159-169
Author(s):  
Benjamin Boettner ◽  
Phoebe Harjes ◽  
Satoshi Ishimaru ◽  
Michael Heke ◽  
Hong Qing Fan ◽  
...  

Abstract Rap1 belongs to the highly conserved Ras subfamily of small GTPases. In Drosophila, Rap1 plays a critical role in many different morphogenetic processes, but the molecular mechanisms executing its function are unknown. Here, we demonstrate that Canoe (Cno), the Drosophila homolog of mammalian junctional protein AF-6, acts as an effector of Rap1 in vivo. Cno binds to the activated form of Rap1 in a yeast two-hybrid assay, the two molecules colocalize to the adherens junction, and they display very similar phenotypes in embryonic dorsal closure (DC), a process that relies on the elongation and migration of epithelial cell sheets. Genetic interaction experiments show that Rap1 and Cno act in the same molecular pathway during DC and that the function of both molecules in DC depends on their ability to interact. We further show that Rap1 acts upstream of Cno, but that Rap1, unlike Cno, is not involved in the stimulation of JNK pathway activity, indicating that Cno has both a Rap1-dependent and a Rap1-independent function in the DC process.


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