title: Conformational mechanism for the stability of microtubule-kinetochore attachments.
abstract: Regulating the stability of microtubule (MT)-kinetochore attachments is fundamental to avoiding mitotic errors and ensuring proper chromosome segregation during cell division. Although biochemical factors involved in this process have been identified, their mechanics still need to be better understood. Here we introduce and simulate a mechanical model of MT-kinetochore interactions in which the stability of the attachment is ruled by the geometrical conformations of curling MT-protofilaments entangled in kinetochore fibrils. The model allows us to reproduce, with good accuracy, in vitro experimental measurements of the detachment times of yeast kinetochores from MTs under external pulling forces. Numerical simulations suggest that geometrical features of MT-protofilaments may play an important role in the switch between stable and unstable attachments.
authors.affiliation: Institute for Scientific Interchange Foundation, Torino, Italy.
authors.forename: Zsolt
authors.initials: Z
authors.lastname: Bertalan
authors.affiliation: Department of Biosciences, University of Milano, Milano, Italy.
authors.forename: Caterina A M
authors.initials: CAM
authors.lastname: La Porta
authors.affiliation: Chromosome Instability and Dynamics Laboratory, Instituto de Biologia Molecular e Celular, University of Porto, Porto, Portugal; Cell Division Unit, Department of Experimental Biology, Faculty of Medicine, University of Porto, Porto, Portugal.
authors.forename: Helder
authors.initials: H
authors.lastname: Maiato
authors.affiliation: Institute for Scientific Interchange Foundation, Torino, Italy; National Research Council of Italy, Istituto per l'Energetica e le Interfasi, Milano, Italy. Electronic address: stefano.zapperi@cnr.it.
authors.forename: Stefano
authors.initials: S
authors.lastname: Zapperi
mesh_terms: D008841:Actin Cytoskeleton / Q000737:chemistry / Q000378:metabolism; D000595:Amino Acid Sequence; D018386:Kinetochores / Q000737:chemistry* / Q000378:metabolism; D008870:Microtubules / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D055550:Protein Stability; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D029701:Saccharomyces cerevisiae Proteins