Dynein-dependent transport of spindle assembly checkpoint proteins off kinetochores toward spindle poles |
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| Authors: | Patrícia MA Silva Rita M Reis Victor M Bolanos-Garcia Claudia Florindo Álvaro A Tavares Hassan Bousbaa |
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| Institution: | 1. CESPU, Instituto de Investigação e Formação Avançada em Ciências e Tecnologias da Saúde, Rua Central de Gandra, 1317, 4585-116 Gandra PRD, Portugal;2. Centre for Molecular and Structural Biomedicine,CBME/IBB, University of Algarve, Faro 8005-139, Portugal;3. Faculty of Health and Life Sciences, Department of Biological and Medical Sciences, Oxford Brookes University, Oxford, United Kingdom;4. Departamento Ciências Biomédicas e Medicina, University of Algarve, Faro 8005-139, Portugal;5. Centro de Química Medicinal da Universidade do Porto (CEQUIMED-UP), Rua de Jorge Viterbo Ferreira 228, 4050-313 Porto, Portugal;6. Centro Interdisciplinar de Investigação Marinha e Ambiental (CIIMAR/CIMAR), Universidade do Porto, Rua dos Bragas 289, 4050-123 Porto, Portugal |
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| Abstract: | A predominant mechanism of spindle assembly checkpoint (SAC) silencing is dynein-mediated transport of certain kinetochore proteins along microtubules. There are still conflicting data as to which SAC proteins are dynein cargoes. Using two ATP reduction assays, we found that the core SAC proteins Mad1, Mad2, Bub1, BubR1, and Bub3 redistributed from attached kinetochores to spindle poles, in a dynein-dependent manner. This redistribution still occurred in metaphase-arrested cells, at a time when the SAC should be satisfied and silenced. Unexpectedly, we found that a pool of Hec1 and Mis12 also relocalizes to spindle poles, suggesting KMN components as additional dynein cargoes. The potential significance of these results for SAC silencing is discussed. |
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| Keywords: | Mitotic checkpoint Checkpoint silencing: cytoplasmic dynein Mad1 Mad2 Bub1 BubR1 Bub3 Hec1 Mis12 |
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