Isoform‐specific interaction of Flamingo/Starry Night with excess Bazooka affects planar cell polarity in the <i>Drosophila</i> wing

Wasserscheid, Isabel; Thomas, Ulrike; Knust, Elisabeth

doi:10.1002/dvdy.21089

Cited by 17 publications

(14 citation statements)

References 44 publications

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“…No interaction was observed between in vitro translated Rbsn-5 and the cytoplasmic tail of both Fmi isoforms (Fmi and Stan) so far described (Wasserscheid et al, 2007) in GST pull-down assays (data not shown). It remains possible that the recruitment of Rbsn-5 by Fmi might require an intermediate binding partner.…”

Section: Flamingo But Neither Strabismus Nor Frizzled Is Rate Limitmentioning

confidence: 82%

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A novel function for the Rab5 effector Rabenosyn-5 in planar cell polarity

et al. 2010

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SUMMARYIn addition to apicobasal polarization, some epithelia also display polarity within the plane of the epithelium. To what extent polarized endocytosis plays a role in the establishment and maintenance of planar cell polarity (PCP) is at present unclear. Here, we investigated the role of Rabenosyn-5 (Rbsn-5), an evolutionarily conserved effector of the small GTPase Rab5, in the development of Drosophila wing epithelium. We found that Rbsn-5 regulates endocytosis at the apical side of the wing epithelium and, surprisingly, further uncovered a novel function of this protein in PCP. At early stages of pupal wing development, the PCP protein Fmi redistributes between the cortex and Rab5-and Rbsn-5-positive early endosomes. During planar polarization, Rbsn-5 is recruited at the apical cell boundaries and redistributes along the proximodistal axis in an Fmidependent manner. At pre-hair formation, Rbsn-5 accumulates at the bottom of emerging hairs. Loss of Rbsn-5 causes intracellular accumulation of Fmi and typical PCP alterations such as defects in cell packing, in the polarized distribution of PCP proteins, and in hair orientation and formation. Our results suggest that establishment of planar polarity requires the activity of Rbsn-5 in regulating both the endocytic trafficking of Fmi at the apical cell boundaries and hair morphology.

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Section: Flamingo But Neither Strabismus Nor Frizzled Is Rate Limitmentioning

confidence: 82%

“…Bound proteins were eluted from the beads, separated by SDS-PAGE and analysed by autoradiography. GST-Fmi and GST-Stan were used as previously described (Wasserscheid et al, 2007).…”

Section: In Vitro Binding Assaymentioning

confidence: 99%

A novel function for the Rab5 effector Rabenosyn-5 in planar cell polarity

et al. 2010

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“…Binding sites have been mapped between Stbm and Pk, as well as between Dsh and Dgo (Jenny et al., 2003, Jenny et al., 2005), and Stbm, Pk, and Dsh contain dimerization motifs (Jenny et al., 2003, Kishida et al., 1999). In addition to this, Fmi, Fz, Stbm, and Dsh contain putative PDZ (PSD-95, Discs Large, ZO-1) binding motifs of unknown function, which may interact with PDZ-containing scaffolding factors (Wolff and Rubin, 1998, Djiane et al., 2005, Wasserscheid et al., 2007, Johnston et al., 2013). Membrane interaction motifs, for example the DEP (Dishevelled, Egl10, and Pleckstrin) domain (Simons et al., 2009) and the Pk prenylation motif (Jenny et al., 2003, Lin and Gubb, 2009, Strutt et al., 2013b), may also promote association of the core proteins to junctions independently of protein-protein interaction sites.…”

Section: Discussionmentioning

confidence: 99%

Robust Asymmetric Localization of Planar Polarity Proteins Is Associated with Organization into Signalosome-like Domains of Variable Stoichiometry

2016

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SummaryIn developing epithelia, the core planar polarity proteins physically interact with each other and localize asymmetrically at opposite cell ends, forming intercellular complexes that link the polarity of neighboring cells. Using quantitative imaging to examine the composition of the core protein complex in vivo, we find that complex composition is unexpectedly plastic. The transmembrane proteins Frizzled and Flamingo form a stoichiometric nucleus in the complex, while the relative levels of the other four core proteins can vary independently. Exploring the functional consequences of this, we show that robust cell polarization is achieved over a range of complex stoichiometries but is dependent on maintaining appropriate levels of the components Frizzled and Strabismus. We propose that the core proteins assemble into signalosome-like structures, where stable association is not dependent on one-to-one interactions with binding partners, and signaling functions can act over a wide range of complex compositions.

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“…However, the interacting Arm isoform ends with –DTDC which does not match any peptides identified, and thus suggests a binding mechanism outside of the peptide binding pockets. Finally, the isoform of Flamingo that was pulled down from cell lysates with the tandem Baz PDZ1-3 protein has a C-terminus of -DDETTV [21], matching all Baz PDZ2 peptides at the P 0 position, and two additionally at the P -3 position and one additionally at the P -5 position. As more proteins are found to interact with Baz, the peptides we have identified will hopefully aid in mapping their specific interaction sites.…”

Section: Discussionmentioning

confidence: 99%

“…Using in vitro binding assays, purified C-terminal portions of the adherens junction components Echinoid and Armadillo ( Drosophila β-catenin) have been shown to bind a purified fusion protein containing all three PDZ domains of Baz in tandem [20]. Also, a purified fusion protein of the three PDZ domains of Baz has been shown to pull down a specific isoform of the atypical cadherin Flamingo from wing imaginal disk extracts [21].…”

Section: Introductionmentioning

confidence: 99%

Peptide Binding Properties of the Three PDZ Domains of Bazooka (Drosophila Par-3)

Tonikian

Felsensteiner

et al. 2014

PLoS ONE

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The Par complex is a conserved cell polarity regulator. Bazooka/Par-3 is scaffold for the complex and contains three PDZ domains in tandem. PDZ domains can act singly or synergistically to bind the C-termini of interacting proteins. Sequence comparisons among Drosophila Baz and its human and C. elegans Par-3 counterparts indicate a divergence of the peptide binding pocket of PDZ1 and greater conservation for the pockets of PDZ2 and PDZ3. However, it is unclear whether the domains from different species share peptide binding preferences, or if their tandem organization affects their peptide binding properties. To investigate these questions, we first used phage display screens to identify unique peptide binding profiles for each single PDZ domain of Baz. Comparisons with published phage display screens indicate that Baz and C. elegans PDZ2 bind to similar peptides, and that the peptide binding preferences of Baz PDZ3 are more similar to C. elegans versus human PDZ3. Next we quantified the peptide binding preferences of each Baz PDZ domain using single identified peptides in surface plasmon resonance assays. In these direct binding studies, each peptide had a binding preference for a single PDZ domain (although the peptide binding of PDZ2 was weakest and the least specific). PDZ1 and PDZ3 bound their peptides with dissociation constants in the nM range, whereas PDZ2-peptide binding was in the µM range. To test whether tandem PDZ domain organization affects peptide binding, we examined a fusion protein containing all three PDZ domains and their normal linker regions. The binding strengths of the PDZ-specific peptides to single PDZ domains and to the PDZ domain tandem were indistinguishable. Thus, the peptide binding pockets of each PDZ domain in Baz are not obviously affected by the presence of neighbouring PDZ domains, but act as isolated modules with specific in vitro peptide binding preferences.

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Isoform‐specific interaction of Flamingo/Starry Night with excess Bazooka affects planar cell polarity in the Drosophila wing

Cited by 17 publications

References 44 publications

A novel function for the Rab5 effector Rabenosyn-5 in planar cell polarity

A novel function for the Rab5 effector Rabenosyn-5 in planar cell polarity

Robust Asymmetric Localization of Planar Polarity Proteins Is Associated with Organization into Signalosome-like Domains of Variable Stoichiometry

Peptide Binding Properties of the Three PDZ Domains of Bazooka (Drosophila Par-3)

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