title: Dynein-dependent transport of spindle assembly checkpoint proteins off kinetochores toward spindle poles.
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.
authors: CESPU, Instituto de Investigação e Formação Avançada em Ciências e Tecnologias da Saúde, Rua Central de Gandra, 1317, 4585-116 Gandra PRD, Portugal; Centre for Molecular and Structural Biomedicine,CBME/IBB, University of Algarve, Faro 8005-139, Portugal.
authors: Patrícia M A
authors: PM
authors: Silva
authors: CESPU, Instituto de Investigação e Formação Avançada em Ciências e Tecnologias da Saúde, Rua Central de Gandra, 1317, 4585-116 Gandra PRD, Portugal.
authors: Rita M
authors: RM
authors: Reis
authors: Faculty of Health and Life Sciences, Department of Biological and Medical Sciences, Oxford Brookes University, Oxford, United Kingdom.
authors: Victor M
authors: VM
authors: Bolanos-Garcia
authors: Centre for Molecular and Structural Biomedicine,CBME/IBB, University of Algarve, Faro 8005-139, Portugal; Departamento Ciências Biomédicas e Medicina, University of Algarve, Faro 8005-139, Portugal.
authors: Claudia
authors: C
authors: Florindo
authors: Centre for Molecular and Structural Biomedicine,CBME/IBB, University of Algarve, Faro 8005-139, Portugal; Departamento Ciências Biomédicas e Medicina, University of Algarve, Faro 8005-139, Portugal.
authors: Álvaro A
authors: ÁA
authors: Tavares
authors: CESPU, Instituto de Investigação e Formação Avançada em Ciências e Tecnologias da Saúde, Rua Central de Gandra, 1317, 4585-116 Gandra PRD, Portugal; Centro de Química Medicinal da Universidade do Porto (CEQUIMED-UP), Rua de Jorge Viterbo Ferreira 228, 4050-313 Porto, Portugal; Centro Interdisciplinar de Investigação Marinha e Ambiental (CIIMAR/CIMAR), Universidade do Porto, Rua dos Bragas 289, 4050-123 Porto, Portugal. Electronic address: hassan.bousbaa@iscsn.cespu.pt.
authors: Hassan
authors: H
authors: Bousbaa
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D018797:Cell Cycle Proteins / Q000172:deficiency / Q000235:genetics / Q000378:metabolism*; D004398:Dyneins / Q000378:metabolism*; D020868:Gene Silencing; D006367:HeLa Cells; D006801:Humans; D018386:Kinetochores / Q000378:metabolism*; D059566:M Phase Cell Cycle Checkpoints; D021381:Protein Transport; D064047:Spindle Poles / Q000378:metabolism*
chemical_list: D018797:Cell Cycle Proteins; D000255:Adenosine Triphosphate; D004398:Dyneins
keywords: Bub1; Bub3; BubR1; Checkpoint silencing: cytoplasmic dynein; Hec1; Mad1; Mad2; Mis12; Mitotic checkpoint