Diego interacts with Prickle and Strabismus/Van Gogh to localize planar cell polarity complexes
Planar cell polarity (PCP) in the Drosophila eye is established by the distinct fate specifications of photoreceptors R3 and R4, and is regulated by the Frizzled (Fz)/PCP signaling pathway. Before the PCP proteins become asymmetrically localized to opposite poles of the cell in response to Fz/PCP si...
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| Veröffentlicht in: | Development (Cambridge) 2004-09, Vol.131 (18), p.4467-4476 |
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| creator | Das, Gishnu Jenny, Andreas Klein, Thomas J Eaton, Suzanne Mlodzik, Marek |
| description | Planar cell polarity (PCP) in the Drosophila eye is established by the distinct fate specifications of photoreceptors R3 and R4, and is regulated by the Frizzled (Fz)/PCP signaling pathway. Before the PCP proteins become asymmetrically localized to opposite poles of the cell in response to Fz/PCP signaling, they are uniformly apically colocalized. Little is known about how the apical localization is maintained. We provide evidence that the PCP protein Diego (Dgo) promotes the maintenance of apical localization of Flamingo (Fmi), an atypical Cadherin-family member, which itself is required for the apical localization of the other PCP factors. This function of Dgo is redundant with Prickle (Pk) and Strabismus (Stbm), and only appreciable in double mutant tissue. We show that the initial membrane association of Dgo depends on Fz, and that Dgo physically interacts with Stbm and Pk through its Ankyrin repeats, providing evidence for a PCP multiprotein complex. These interactions suggest a positive feedback loop initiated by Fz that results in the apical maintenance of other PCP factors through Fmi. |
| doi_str_mv | 10.1242/dev.01317 |
| format | Article |
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Before the PCP proteins become asymmetrically localized to opposite poles of the cell in response to Fz/PCP signaling, they are uniformly apically colocalized. Little is known about how the apical localization is maintained. We provide evidence that the PCP protein Diego (Dgo) promotes the maintenance of apical localization of Flamingo (Fmi), an atypical Cadherin-family member, which itself is required for the apical localization of the other PCP factors. This function of Dgo is redundant with Prickle (Pk) and Strabismus (Stbm), and only appreciable in double mutant tissue. We show that the initial membrane association of Dgo depends on Fz, and that Dgo physically interacts with Stbm and Pk through its Ankyrin repeats, providing evidence for a PCP multiprotein complex. 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These interactions suggest a positive feedback loop initiated by Fz that results in the apical maintenance of other PCP factors through Fmi.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Animals</subject><subject>Cadherins - metabolism</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Polarity</subject><subject>Cell Size</subject><subject>Dishevelled Proteins</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Drosophila - cytology</subject><subject>Drosophila - embryology</subject><subject>Drosophila - genetics</subject><subject>Drosophila - metabolism</subject><subject>Drosophila Proteins - genetics</subject><subject>Drosophila Proteins - metabolism</subject><subject>Frizzled Receptors</subject><subject>LIM Domain Proteins</subject><subject>Membrane Proteins - metabolism</subject><subject>Phenotype</subject><subject>Phosphoproteins - metabolism</subject><subject>Protein Binding</subject><subject>Protein Transport</subject><subject>Receptors, G-Protein-Coupled</subject><subject>Signal Transduction</subject><issn>0950-1991</issn><issn>1477-9129</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1P3DAQQK0K1F1oD_yByiekHrL4I7HjYwVlQUKiUmmvluNMdk2dOLW9bOHXk2VX4tjTXN68GT2EzihZUFayixaeFoRyKj-gOS2lLBRl6gjNiapIQZWiM3SS0iMhhAspP6IZrTgRlZBzpK8crAJ2Q4ZobE546_Ia_4jO_vGAzdDinzmaxqV-ky5-mwEvw2qNc8A-WOPdC-DRm8FEbMF7PAZvosvP2IZ-9PAP0id03Bmf4PNhnqJf198fLm-Ku_vl7eW3u8LyWuRCcF52Da8bRYDYRrBSEs6qGhQ3bWsroxirRddJLpmsqloaI1ijZAc1a4lU_BSd771jDH83kLLuXdr9ZAYIm6SFqLmUpPwvSGtSSiqqCfy6B20MKUXo9Bhdb-KzpkTvsuspu37LPrFfDtJN00P7Th46T8BiD6zdar11EXTjgg8rl3LaecCHUU-q6bwuy2nhFV9cjZU</recordid><startdate>20040901</startdate><enddate>20040901</enddate><creator>Das, Gishnu</creator><creator>Jenny, Andreas</creator><creator>Klein, Thomas J</creator><creator>Eaton, Suzanne</creator><creator>Mlodzik, Marek</creator><general>The Company of Biologists Limited</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7SS</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20040901</creationdate><title>Diego interacts with Prickle and Strabismus/Van Gogh to localize planar cell polarity complexes</title><author>Das, Gishnu ; Jenny, Andreas ; Klein, Thomas J ; Eaton, Suzanne ; Mlodzik, Marek</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-6334fb38b90e0cb624703258e93addc5a92286ff737275587aa62b97fe82d0793</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Adaptor Proteins, Signal Transducing</topic><topic>Animals</topic><topic>Cadherins - metabolism</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Polarity</topic><topic>Cell Size</topic><topic>Dishevelled Proteins</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Drosophila - cytology</topic><topic>Drosophila - embryology</topic><topic>Drosophila - genetics</topic><topic>Drosophila - metabolism</topic><topic>Drosophila Proteins - genetics</topic><topic>Drosophila Proteins - metabolism</topic><topic>Frizzled Receptors</topic><topic>LIM Domain Proteins</topic><topic>Membrane Proteins - metabolism</topic><topic>Phenotype</topic><topic>Phosphoproteins - metabolism</topic><topic>Protein Binding</topic><topic>Protein Transport</topic><topic>Receptors, G-Protein-Coupled</topic><topic>Signal Transduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Das, Gishnu</creatorcontrib><creatorcontrib>Jenny, Andreas</creatorcontrib><creatorcontrib>Klein, Thomas J</creatorcontrib><creatorcontrib>Eaton, Suzanne</creatorcontrib><creatorcontrib>Mlodzik, Marek</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Development (Cambridge)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Das, Gishnu</au><au>Jenny, Andreas</au><au>Klein, Thomas J</au><au>Eaton, Suzanne</au><au>Mlodzik, Marek</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Diego interacts with Prickle and Strabismus/Van Gogh to localize planar cell polarity complexes</atitle><jtitle>Development (Cambridge)</jtitle><addtitle>Development</addtitle><date>2004-09-01</date><risdate>2004</risdate><volume>131</volume><issue>18</issue><spage>4467</spage><epage>4476</epage><pages>4467-4476</pages><issn>0950-1991</issn><eissn>1477-9129</eissn><abstract>Planar cell polarity (PCP) in the Drosophila eye is established by the distinct fate specifications of photoreceptors R3 and R4, and is regulated by the Frizzled (Fz)/PCP signaling pathway. Before the PCP proteins become asymmetrically localized to opposite poles of the cell in response to Fz/PCP signaling, they are uniformly apically colocalized. Little is known about how the apical localization is maintained. We provide evidence that the PCP protein Diego (Dgo) promotes the maintenance of apical localization of Flamingo (Fmi), an atypical Cadherin-family member, which itself is required for the apical localization of the other PCP factors. This function of Dgo is redundant with Prickle (Pk) and Strabismus (Stbm), and only appreciable in double mutant tissue. We show that the initial membrane association of Dgo depends on Fz, and that Dgo physically interacts with Stbm and Pk through its Ankyrin repeats, providing evidence for a PCP multiprotein complex. 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| ispartof | Development (Cambridge), 2004-09, Vol.131 (18), p.4467-4476 |
| issn | 0950-1991 1477-9129 |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection; Company of Biologists |
| subjects | Adaptor Proteins, Signal Transducing Animals Cadherins - metabolism Carrier Proteins - genetics Carrier Proteins - metabolism Cell Polarity Cell Size Dishevelled Proteins DNA-Binding Proteins - metabolism Drosophila - cytology Drosophila - embryology Drosophila - genetics Drosophila - metabolism Drosophila Proteins - genetics Drosophila Proteins - metabolism Frizzled Receptors LIM Domain Proteins Membrane Proteins - metabolism Phenotype Phosphoproteins - metabolism Protein Binding Protein Transport Receptors, G-Protein-Coupled Signal Transduction |
| title | Diego interacts with Prickle and Strabismus/Van Gogh to localize planar cell polarity complexes |
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