The Autosomal FLP-DFS Technique for Generating Germline Mosaics in <i>Drosophila melanogaster</i>

Chou, Tze-Bin; Perrimon, Norbert

doi:10.1093/genetics/144.4.1673

Cited by 617 publications

(94 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The UAS-GAL4 system was employed to drive the expression of transgenes ( Brand et al, 1994 ). Mosaic analysis in the follicular epithelium was performed using the Flippase recognition target (FRT)/Flippase (FLP) system in which the FLP recombinase was under the control of a heat shock promoter ( hsFLP ) ( Chou and Perrimon, 1996 ; Golic and Lindquist, 1989 ). Newly hatched females were heat-shocked for 3 hr at 37°C on two consecutive days.…”

Section: Methodsmentioning

confidence: 99%

Pak1 and PP2A antagonize aPKC function to support cortical tension induced by the Crumbs-Yurt complex

Biehler

Rothenberg

Jetté

et al. 2021

eLife

View full text Add to dashboard Cite

The Drosophila polarity protein Crumbs is essential for the establishment and growth of the apical domain in epithelial cells. The protein Yurt limits the ability of Crumbs to promote apical membrane growth, thereby defining proper apical/lateral membrane ratio that is crucial for forming and maintaining complex epithelial structures such as tubes or acini. Here, we show that Yurt also increases Myosin-dependent cortical tension downstream of Crumbs. Yurt overexpression thus induces apical constriction in epithelial cells. The kinase aPKC phosphorylates Yurt, thereby dislodging the latter from the apical domain and releasing apical tension. In contrast, the kinase Pak1 promotes Yurt dephosphorylation through activation of the phosphatase PP2A. The Pak1-PP2A module thus opposes aPKC function and supports Yurt-induced apical constriction. Hence, the complex interplay between Yurt, aPKC, Pak1 and PP2A contributes to the functional plasticity of Crumbs. Overall, our data increase our understanding of how proteins sustaining epithelial cell polarization and Myosin-dependent cell contractility interact with one another to control epithelial tissue architecture.

show abstract

Section: Methodsmentioning

confidence: 99%

Pak1 and PP2A antagonize aPKC function to support cortical tension induced by the Crumbs-Yurt complex

Biehler

Rothenberg

Jetté

et al. 2021

eLife

View full text Add to dashboard Cite

show abstract

“…Rescue crosses were performed by crossing Twi-GAL4, sltr/CyO, actin-lacZ with UAS-sltr, sltr/CyO, actin-lacZ or UAS-''sltr mutant,'' sltr/CyO, actin-lacZ, in which ''sltr mutant'' represents sltrDWH2-1&2, sltrDWH2-1, sltrK49Q, sltrDWH2-2, or sltrDWBD. Wasp germline clones were generated using the FLP/FRT system as described (Chou and Perrimon, 1996). For the GFP diffusion assay, rP298-GAL4; sltr S1946 /CyO males were crossed with sltr S1946 , UAS-GFP/CyO females.…”

Section: Fly Geneticsmentioning

confidence: 99%

A Critical Function for the Actin Cytoskeleton in Targeted Exocytosis of Prefusion Vesicles during Myoblast Fusion

et al. 2007

View full text Add to dashboard Cite

Myoblast fusion is an essential step during muscle differentiation. Previous studies in Drosophila have revealed a signaling pathway that relays the fusion signal from the plasma membrane to the actin cytoskeleton. However, the function for the actin cytoskeleton in myoblast fusion remains unclear. Here we describe the characterization of solitary (sltr), a component of the myoblast fusion signaling cascade. sltr encodes the Drosophila ortholog of the mammalian WASP-interacting protein. Sltr is recruited to sites of fusion by the fusion-competent cell-specific receptor Sns and acts as a positive regulator for actin polymerization at these sites. Electron microscopy analysis suggests that formation of F-actin-enriched foci at sites of fusion is involved in the proper targeting and coating of prefusion vesicles. These studies reveal a surprising cell-type specificity of Sltr-mediated actin polymerization in myoblast fusion, and demonstrate that targeted exocytosis of prefusion vesicles is a critical step prior to plasma membrane fusion.

show abstract

“…Germline clones and somatic clones were generated by FRT-FLP recombination (Golic, 1991;Xu and Rubin, 1993;Chou and Perrimon, 1996). The genotypes used in our analyses were as follows:…”

Section: Generation Of Germline Clones and Marked Wing Clonesmentioning

confidence: 99%

The Ihog Cell-Surface Proteins Bind Hedgehog and Mediate Pathway Activation

Yao

Lum

Beachy

2006

Cell

206

238

View full text Add to dashboard Cite

The ihog gene (interference hedgehog), identified by RNA interference in Drosophila cultured cells, encodes a type 1 membrane protein shown here to bind and to mediate response to the active Hedgehog (Hh) protein signal. ihog mutations produce defects characteristic of Hh signaling loss in embryos and imaginal discs, and epistasis analysis places ihog action at or upstream of the negatively acting receptor component, Patched (Ptc). The first of two extracellular fibronectin type III (FNIII) domains of the Ihog protein mediates a specific interaction with Hh protein in vitro, but the second FNIII domain is additionally required for in vivo signaling activity and for Ihog-enhanced binding of Hh protein to cells coexpressing Ptc. Other members of the Ihog family, including Drosophila Boi and mammalian CDO and BOC, also interact with Hh ligands via a specific FNIII domain, thus identifying an evolutionarily conserved family of membrane proteins that function in Hh signal response.

show abstract

The Autosomal FLP-DFS Technique for Generating Germline Mosaics in Drosophila melanogaster

Cited by 617 publications

References 13 publications

Pak1 and PP2A antagonize aPKC function to support cortical tension induced by the Crumbs-Yurt complex

Pak1 and PP2A antagonize aPKC function to support cortical tension induced by the Crumbs-Yurt complex

A Critical Function for the Actin Cytoskeleton in Targeted Exocytosis of Prefusion Vesicles during Myoblast Fusion

The Ihog Cell-Surface Proteins Bind Hedgehog and Mediate Pathway Activation

Contact Info

Product

Resources

About