Interactome and F-Actin Interaction Analysis of <i>Dictyostelium discoideum</i> Coronin A
Coronin proteins are evolutionary conserved WD repeat containing proteins that have been proposed to carry out different functions. In <i>Dictyostelium</i>, the short coronin isoform, coronin A, has been implicated in cytoskeletal reorganization, chemotaxis, phagocytosis and the initiati...
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2020-02-01
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| Series: | International Journal of Molecular Sciences |
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| author | Tohnyui Ndinyanka Fabrice Thomas Fiedler Vera Studer Adrien Vinet Francesco Brogna Alexander Schmidt Jean Pieters |
| author_facet | Tohnyui Ndinyanka Fabrice Thomas Fiedler Vera Studer Adrien Vinet Francesco Brogna Alexander Schmidt Jean Pieters |
| author_sort | Tohnyui Ndinyanka Fabrice |
| collection | DOAJ |
| description | Coronin proteins are evolutionary conserved WD repeat containing proteins that have been proposed to carry out different functions. In <i>Dictyostelium</i>, the short coronin isoform, coronin A, has been implicated in cytoskeletal reorganization, chemotaxis, phagocytosis and the initiation of multicellular development. Generally thought of as modulators of F-actin, coronin A and its mammalian homologs have also been shown to mediate cellular processes in an F-actin-independent manner. Therefore, it remains unclear whether or not coronin A carries out its functions through its capacity to interact with F-actin. Moreover, the interacting partners of coronin A are not known. Here, we analyzed the interactome of coronin A as well as its interaction with F-actin within cells and in vitro. Interactome analysis showed the association with a diverse set of interaction partners, including fimbrin, talin and myosin subunits, with only a transient interaction with the minor actin10 isoform, but not the major form of actin, actin8, which was consistent with the absence of a coronin A-actin interaction as analyzed by co-sedimentation from cells and lysates. In vitro, however, purified coronin A co-precipitated with rabbit muscle F-actin in a coiled-coil-dependent manner. Our results suggest that an in vitro interaction of coronin A and rabbit muscle actin may not reflect the cellular interaction state of coronin A with actin, and that coronin A interacts with diverse proteins in a time-dependent manner. |
| first_indexed | 2024-04-13T17:01:01Z |
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| issn | 1422-0067 |
| language | English |
| last_indexed | 2024-04-13T17:01:01Z |
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| series | International Journal of Molecular Sciences |
| spelling | doaj.art-ffd58ba037ae43d5b6354d5de958bf752022-12-22T02:38:39ZengMDPI AGInternational Journal of Molecular Sciences1422-00672020-02-01214146910.3390/ijms21041469ijms21041469Interactome and F-Actin Interaction Analysis of <i>Dictyostelium discoideum</i> Coronin ATohnyui Ndinyanka Fabrice0Thomas Fiedler1Vera Studer2Adrien Vinet3Francesco Brogna4Alexander Schmidt5Jean Pieters6Biozentrum, University of Basel, Klingelbergstrasse 50, 4056 Basel, SwitzerlandBiozentrum, University of Basel, Klingelbergstrasse 50, 4056 Basel, SwitzerlandBiozentrum, University of Basel, Klingelbergstrasse 50, 4056 Basel, SwitzerlandBiozentrum, University of Basel, Klingelbergstrasse 50, 4056 Basel, SwitzerlandBiozentrum, University of Basel, Klingelbergstrasse 50, 4056 Basel, SwitzerlandBiozentrum, University of Basel, Klingelbergstrasse 50, 4056 Basel, SwitzerlandBiozentrum, University of Basel, Klingelbergstrasse 50, 4056 Basel, SwitzerlandCoronin proteins are evolutionary conserved WD repeat containing proteins that have been proposed to carry out different functions. In <i>Dictyostelium</i>, the short coronin isoform, coronin A, has been implicated in cytoskeletal reorganization, chemotaxis, phagocytosis and the initiation of multicellular development. Generally thought of as modulators of F-actin, coronin A and its mammalian homologs have also been shown to mediate cellular processes in an F-actin-independent manner. Therefore, it remains unclear whether or not coronin A carries out its functions through its capacity to interact with F-actin. Moreover, the interacting partners of coronin A are not known. Here, we analyzed the interactome of coronin A as well as its interaction with F-actin within cells and in vitro. Interactome analysis showed the association with a diverse set of interaction partners, including fimbrin, talin and myosin subunits, with only a transient interaction with the minor actin10 isoform, but not the major form of actin, actin8, which was consistent with the absence of a coronin A-actin interaction as analyzed by co-sedimentation from cells and lysates. In vitro, however, purified coronin A co-precipitated with rabbit muscle F-actin in a coiled-coil-dependent manner. Our results suggest that an in vitro interaction of coronin A and rabbit muscle actin may not reflect the cellular interaction state of coronin A with actin, and that coronin A interacts with diverse proteins in a time-dependent manner.https://www.mdpi.com/1422-0067/21/4/1469<i>dictyostelium</i>coronin ainteractome analysisactin |
| spellingShingle | Tohnyui Ndinyanka Fabrice Thomas Fiedler Vera Studer Adrien Vinet Francesco Brogna Alexander Schmidt Jean Pieters Interactome and F-Actin Interaction Analysis of <i>Dictyostelium discoideum</i> Coronin A International Journal of Molecular Sciences <i>dictyostelium</i> coronin a interactome analysis actin |
| title | Interactome and F-Actin Interaction Analysis of <i>Dictyostelium discoideum</i> Coronin A |
| title_full | Interactome and F-Actin Interaction Analysis of <i>Dictyostelium discoideum</i> Coronin A |
| title_fullStr | Interactome and F-Actin Interaction Analysis of <i>Dictyostelium discoideum</i> Coronin A |
| title_full_unstemmed | Interactome and F-Actin Interaction Analysis of <i>Dictyostelium discoideum</i> Coronin A |
| title_short | Interactome and F-Actin Interaction Analysis of <i>Dictyostelium discoideum</i> Coronin A |
| title_sort | interactome and f actin interaction analysis of i dictyostelium discoideum i coronin a |
| topic | <i>dictyostelium</i> coronin a interactome analysis actin |
| url | https://www.mdpi.com/1422-0067/21/4/1469 |
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