The fission yeast septation initiation network (SIN) kinase, Sid2, is required for SIN asymmetry and regulates the SIN scaffold, Cdc11
| Autor: | Jennifer L. Morrell-Falvey, Kathleen L. Gould, Anna Feoktistova, Mohan K. Balasubramanian, Jun-Song Chen, N. Sadananda Singh |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
Scaffold protein
genetic structures viruses Mitosis Cell Cycle Proteins Protein Serine-Threonine Kinases Spindle pole body 03 medical and health sciences 0302 clinical medicine Schizosaccharomyces Phosphorylation Protein kinase A Molecular Biology 030304 developmental biology Anaphase 0303 health sciences biology Cell Cycle food and beverages virus diseases Cell Biology Articles biochemical phenomena metabolism and nutrition biology.organism_classification 3. Good health Cell biology Schizosaccharomyces pombe Schizosaccharomyces pombe Proteins Signal transduction Protein Kinases Protein Processing Post-Translational 030217 neurology & neurosurgery Signal Transduction |
| Zdroj: | Molecular Biology of the Cell |
| ISSN: | 1939-4586 1059-1524 |
| Popis: | Some components of the fission yeast septation initiation network (SIN) localize asymmetrically to spindle pole bodies during anaphase. Symmetric localization of these proteins correlates with cytokinesis defects. It is shown that the SIN-kinase Sid2 mediates SIN asymmetry, in part via the scaffold Cdc11, revealing a previously unknown feedback loop operating to generate SIN asymmetry. The Schizosaccharomyces pombe septation initiation network (SIN) is an Spg1-GTPase–mediated protein kinase cascade that triggers actomyosin ring constriction, septation, and cell division. The SIN is assembled at the spindle pole body (SPB) on the scaffold proteins Cdc11 and Sid4, with Cdc11 binding directly to SIN signaling components. Proficient SIN activity requires the asymmetric distribution of its signaling components to one of the two SPBs during anaphase, and Cdc11 hyperphosphorylation correlates with proficient SIN activity. In this paper, we show that the last protein kinase in the signaling cascade, Sid2, feeds back to phosphorylate Cdc11 during mitosis. The characterization of Cdc11 phosphomutants provides evidence that Sid2-mediated Cdc11 phosphorylation promotes the association of the SIN kinase, Cdc7, with the SPB and maximum SIN signaling during anaphase. We also show that Sid2 is crucial for the establishment of SIN asymmetry, indicating a positive-feedback loop is an important element of the SIN. |
| Databáze: | OpenAIRE |
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