Apical Accumulation of the Sevenless Receptor Tyrosine Kinase During <i>Drosophila</i> Eye Development Is Promoted by the Small GTPase Rap1

Baril, Caroline; Lefrançois, Martin; Sahmi, Malha; Therrien, Marc

doi:10.1534/genetics.114.166272

Cited by 9 publications

(6 citation statements)

References 84 publications

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“…All of these defects were milder than those reported for alleles that more severely disrupt cno , and defects were substantially more penetrant in cnoΔPDZ than cnoΔFAB retinas, suggesting different utilization of the PDZ and FAB domains of Cno in the eye versus embryo. The defects we observed in the pupal eye were qualitatively similar to those reported when expression of Cno regulators or Cno-binding proteins was reduced, including Rap1, Dizzy, Pyd, and Sdk ( Baril et al, 2014 ; Chen et al, 1996 ; Letizia et al, 2019 ; Nguyen et al, 1997 ; O’Keefe et al, 2009 ; Seppa et al, 2008 ; Walther et al, 2018 ).…”

Section: Resultssupporting

confidence: 80%

Multivalent interactions make adherens junction–cytoskeletal linkage robust during morphogenesis

Perez-Vale

Yow

Johnson

et al. 2021

Journal of Cell Biology

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Embryogenesis requires cells to change shape and move without disrupting epithelial integrity. This requires robust, responsive linkage between adherens junctions and the actomyosin cytoskeleton. Using Drosophila morphogenesis, we define molecular mechanisms mediating junction–cytoskeletal linkage and explore the role of mechanosensing. We focus on the junction–cytoskeletal linker Canoe, a multidomain protein. We engineered the canoe locus to define how its domains mediate its mechanism of action. To our surprise, the PDZ and FAB domains, which we thought connected junctions and F-actin, are not required for viability or mechanosensitive recruitment to junctions under tension. The FAB domain stabilizes junctions experiencing elevated force, but in its absence, most cells recover, suggesting redundant interactions. In contrast, the Rap1-binding RA domains are critical for all Cno functions and enrichment at junctions under tension. This supports a model in which junctional robustness derives from a large protein network assembled via multivalent interactions, with proteins at network nodes and some node connections more critical than others.

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Section: Resultssupporting

confidence: 80%

Multivalent interactions make adherens junction–cytoskeletal linkage robust during morphogenesis

Perez-Vale

Yow

Johnson

et al. 2021

Journal of Cell Biology

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“…However, an alternative model is that RAP-1 acts to reinforce other aspects of the 1°-promoting signal. For example, RAP-1 could promote or stabilize EGFR signaling, as Drosophila Rap1 has been shown to regulate EGFR membrane localization and polarity through its junctional effector Canoe/afadin/AF6 (O'Keefe et al 2009;Baril et al 2014). Such a function, piggybacking on the strong induction of 1°cells by LET-60, could induce occasional ectopic 1°cells.…”

Section: Discussionmentioning

confidence: 99%

“…Studies in Drosophila suggest that Rap1 is necessary for maximal induction of the Raf-MEK-ERK MAP kinase cascade, perhaps in parallel to Ras activation (Mishra et al 2005;Mavromatakis and Tomlinson 2012). Yet also in Drosophila, results with Rap1 have been contradictory (Baril et al 2014). The Drosophila Roughened mutation, originally thought to be a hypermorphic allele, was subsequently inferred to be a dominant-negative mutation (Hariharan et al 1991;Mavromatakis and Tomlinson 2012).…”

mentioning

confidence: 99%

Ras-Dependent Cell Fate Decisions Are Reinforced by the RAP-1 Small GTPase in Caenorhabditis elegans

2018

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The notoriety of the small GTPase Ras as the most mutated oncoprotein has led to a well-characterized signaling network largely conserved across metazoans. Yet the role of its close relative Rap1 (Ras Proximal), which shares 100% identity between their core effector binding sequences, remains unclear. A long-standing controversy in the field is whether Rap1 also functions to activate the canonical Ras effector, the S/T kinase Raf. We used the developmentally simpler Caenorhabditis elegans, which lacks the extensive paralog redundancy of vertebrates, to examine the role of RAP-1 in two distinct LET-60/Ras-dependent cell fate patterning events: induction of 1°vulval precursor cell (VPC) fate and of the excretory duct cell. Fluorescence-tagged endogenous RAP-1 is localized to plasma membranes and is expressed ubiquitously, with even expression levels across the VPCs. RAP-1 and its activating GEF PXF-1 function cell autonomously and are necessary for maximal induction of 1°VPCs. Critically, mutationally activated endogenous RAP-1 is sufficient both to induce ectopic 1°s and duplicate excretory duct cells. Like endogenous RAP-1, before induction GFP expression from the pxf-1 promoter is uniform across VPCs. However, unlike endogenous RAP-1, after induction GFP expression is increased in presumptive 1°s and decreased in presumptive 2°s. We conclude that RAP-1 is a positive regulator that promotes Ras-dependent inductive fate decisions. We hypothesize that PXF-1 activation of RAP-1 serves as a minor parallel input into the major LET-60/Ras signal through LIN-45/Raf.

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“…Although all photoreceptor cells express a minimum of N-Cad, only the AJ between R3 and R4 accumulate N-Cad (Mirkovic and Mlodzik, 2006). In this context, enrichment of E-Cad at the AJ, but not of N-Cad, depends on Rap1 signaling (Baril et al, 2014; O'Keefe et al, 2009). The mechanism of how N-Cad AJ between R3 and R4 are established and maintained is unknown.…”

Section: Introductionmentioning

confidence: 99%

Mbt/PAK4 together with SRC modulates N-Cadherin adherens junctions in the developingDrosophilaeye

Pütz

2019

Biology Open

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Tissue morphogenesis is accompanied by changes of adherens junctions (AJ). During Drosophila eye development, AJ reorganization includes the formation of isolated N-Cadherin AJ between photoreceptors R3/R4. Little is known about how these N-Cadherin AJ are established and maintained. This study focuses on the kinases Mbt/PAK4 and SRC, both known to alter E-Cadherin AJ across phyla. Drosophila p21-activated kinase Mbt and the non-receptor tyrosine kinases Src64 and Src42 regulate proper N-Cadherin AJ. N-Cadherin AJ elongation depends on SRC kinase activity. Cell culture experiments demonstrate binding of both Drosophila SRC isoforms to N-Cadherin and its subsequent tyrosine phosphorylation. In contrast, Mbt stabilizes but does not bind N-Cadherin in vitro . Mbt is required in R3/R4 for zipping the N-Cadherin AJ between these cells, independent of its kinase activity and Cdc42-binding. The mbt phenotype can be reverted by mutations in Src64 and Src42 . Because Mbt neither directly binds to SRC proteins nor has a reproducible influence on their kinase activity, the conclusion is that Mbt and SRC signaling converge on N-Cadherin. N-Cadherin AJ formation during eye development requires a proper balance between the promoting effects of Mbt and the inhibiting influences of SRC kinases.

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Apical Accumulation of the Sevenless Receptor Tyrosine Kinase During Drosophila Eye Development Is Promoted by the Small GTPase Rap1

Cited by 9 publications

References 84 publications

Multivalent interactions make adherens junction–cytoskeletal linkage robust during morphogenesis

Multivalent interactions make adherens junction–cytoskeletal linkage robust during morphogenesis

Ras-Dependent Cell Fate Decisions Are Reinforced by the RAP-1 Small GTPase in Caenorhabditis elegans

Mbt/PAK4 together with SRC modulates N-Cadherin adherens junctions in the developingDrosophilaeye

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