Interactome and F-Actin Interaction Analysis of Dictyostelium discoideum Coronin A
| العنوان: | Interactome and F-Actin Interaction Analysis of Dictyostelium discoideum Coronin A |
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| المؤلفون: | Jean Pieters, Adrien F. Vinet, Thomas Fiedler, Vera Studer, Alexander Schmidt, Tohnyui Ndinyanka Fabrice, Francesco Brogna |
| المصدر: | International Journal of Molecular Sciences, Vol 21, Iss 4, p 1469 (2020) International Journal of Molecular Sciences Volume 21 Issue 4 |
| بيانات النشر: | MDPI AG, 2020. |
| سنة النشر: | 2020 |
| مصطلحات موضوعية: | 0301 basic medicine, Protozoan Proteins, Coronin, macromolecular substances, Interactome, Article, Catalysis, Dictyostelium discoideum, lcsh:Chemistry, Inorganic Chemistry, 03 medical and health sciences, Myosin, Animals, Dictyostelium, Physical and Theoretical Chemistry, lcsh:QH301-705.5, Molecular Biology, coronin a, Spectroscopy, Actin, 030102 biochemistry & molecular biology, biology, Chemistry, Microfilament Proteins, Organic Chemistry, Chemotaxis, General Medicine, biology.organism_classification, Actins, Computer Science Applications, Cell biology, 030104 developmental biology, lcsh:Biology (General), lcsh:QD1-999, Fimbrin, biology.protein, interactome analysis, Rabbits, dictyostelium, actin |
| الوصف: | Coronin proteins are evolutionary conserved WD repeat containing proteins that have been proposed to carry out different functions. In Dictyostelium, 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. |
| وصف الملف: | application/pdf |
| تدمد: | 1422-0067 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d4293c320fa81165219746a2128c5edTest https://doi.org/10.3390/ijms21041469Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....5d4293c320fa81165219746a2128c5ed |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14220067 |
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