SSBD:database

Shuhei Yoshida, Masako Kaido, Tomoya S Kitajima (2015) Inherent Instability of Correct Kinetochore-Microtubule Attachments during Meiosis I in Oocytes., Developmental cell, Volume 33, Number 5, pp. 589-602

Published in 2015 Jun 8 (Electronic publication in May 28, 2015, midnight )

• doi: 10.1016/j.devcel.2015.04.020
• pmid: 26028219
  

(Abstract) A model for mitosis suggests that correct kinetochore-microtubule (KT-MT) attachments are stabilized by spatial separation of the attachment sites from Aurora B kinase through sister KT stretching. However, the spatiotemporal regulation of attachment stability during meiosis I (MI) in oocytes remains unclear. Here, we found that in mouse oocytes, Aurora B and C (B/C) are located in close proximity to KT-MT attachment sites after bivalent stretching due to an intrinsic property of the MI chromosomes. The Aurora B/C activity destabilizes correct attachments while allowing a considerable amount of incorrect attachments to form. KT-MT attachments are eventually stabilized through KT dephosphorylation by PP2A-B56 phosphatase, which is progressively recruited to KTs depending on the BubR1 phosphorylation resulting from the timer Cdk1 and independent of bivalent stretching. Thus, oocytes lack a mechanism for coordinating bivalent stretching and KT phosphoregulation during MI, which may explain the high frequency of KT-MT attachment errors.

• Animals
• Aurora Kinase B/metabolism
• Aurora Kinase C/metabolism
• CDC2 Protein Kinase/metabolism
• Cell Cycle Proteins/metabolism
• Chromosome Segregation[major]
• Female
• Fluorescent Antibody Technique
• Image Processing, Computer-Assisted
• Kinetochores/physiology[major]
• Meiosis/physiology[major]
• Mice
• Microtubules/physiology[major]
• Oocytes/cytology
• Oocytes/metabolism[major]
• Phosphorylation
• Protein Phosphatase 2/metabolism
• Protein Serine-Threonine Kinases/metabolism