دورية أكاديمية
The substrate of Greatwall kinase, Arpp19, controls mitosis by inhibiting protein phosphatase 2A.
| العنوان: | The substrate of Greatwall kinase, Arpp19, controls mitosis by inhibiting protein phosphatase 2A. |
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| المؤلفون: | Gharbi-Ayachi, Aicha, Labbé, Jean-Claude, Burgess, Andrew, Vigneron, Suzanne, Strub, Jean-Marc, Brioudes, Estelle, Van-Dorsselaer, Alain, Castro, Anna, Lorca, Thierry |
| المساهمون: | Centre de recherche en Biologie Cellulaire (CRBM), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Institut Pluridisciplinaire Hubert Curien (IPHC), Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS) |
| المصدر: | ISSN: 0036-8075. |
| بيانات النشر: | HAL CCSD American Association for the Advancement of Science (AAAS) |
| سنة النشر: | 2010 |
| المجموعة: | HAL-IN2P3 (Institut national de physique nucléaire et de physique des particules) |
| مصطلحات موضوعية: | MESH: Amino Acid Sequence, MESH: Animals, MESH: Phosphorylation, MESH: Protein Binding, MESH: Protein Phosphatase 2, MESH: Protein-Serine-Threonine Kinases, MESH: Proto-Oncogene Proteins c-mos, MESH: Recombinant Fusion Proteins, MESH: Xenopus Proteins, MESH: Xenopus laevis, MESH: Hela Cells, MESH: Humans, MESH: Interphase, MESH: Mitosis, MESH: Molecular Sequence Data, MESH: Oocytes, MESH: Peptides, MESH: Phosphoproteins, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology |
| الوصف: | International audience ; Initiation and maintenance of mitosis require the activation of protein kinase cyclin B-Cdc2 and the inhibition of protein phosphatase 2A (PP2A), which, respectively, phosphorylate and dephosphorylate mitotic substrates. The protein kinase Greatwall (Gwl) is required to maintain mitosis through PP2A inhibition. We describe how Gwl activation results in PP2A inhibition. We identified cyclic adenosine monophosphate-regulated phosphoprotein 19 (Arpp19) and α-Endosulfine as two substrates of Gwl that, when phosphorylated by this kinase, associate with and inhibit PP2A, thus promoting mitotic entry. Conversely, in the absence of Gwl activity, Arpp19 and α-Endosulfine are dephosphorylated and lose their capacity to bind and inhibit PP2A. Although both proteins can inhibit PP2A, endogenous Arpp19, but not α-Endosulfine, is responsible for PP2A inhibition at mitotic entry in Xenopus egg extracts. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| العلاقة: | info:eu-repo/semantics/altIdentifier/pmid/21164014; hal-00556511; https://hal.science/hal-00556511Test; https://hal.science/hal-00556511/documentTest; https://hal.science/hal-00556511/file/2010TLorca_The%20Substrate%20of%20Greatwall.pdfTest; PUBMED: 21164014 |
| DOI: | 10.1126/science.1197048 |
| الإتاحة: | https://doi.org/10.1126/science.1197048Test https://hal.science/hal-00556511Test https://hal.science/hal-00556511/documentTest https://hal.science/hal-00556511/file/2010TLorca_The%20Substrate%20of%20Greatwall.pdfTest |
| حقوق: | info:eu-repo/semantics/OpenAccess |
| رقم الانضمام: | edsbas.FDBF5D28 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1126/science.1197048 |
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