Detail of FigureS3D_140511_B56e_ACA_control_120min



Project
Title
Timelapse confocal images of oocytes epressing 3mEGFP-PP22A-B56e cultured in control medium for 120 minutes (choromosome: blue)
Description
Timelapse confocal images of oocytes epressing 3mEGFP-PP22A-B56e cultured in control medium for 120 minutes (choromosome: blue)
Release, Updated
2021-09-30
License
CC BY
Kind
Image data
File Formats
Data size
338.7 MB

Organism
Mus musculus ( NCBI:txid10090 )
Strain(s)
-
Cell Line
-
Protein names
PP22A
Protein tags
3mEGFP

Datatype
-
Molecular Function (MF)
-
Biological Process (BP)
mitotic cell cycle ( GO:0007067 )
Cellular Component (CC)
kinetochore microtubule ( GO:0005828 ) chromosome ( GO:0005694 )
Biological Imaging Method
time lapse microscopy ( Fbbi:00000249 )
X scale
0.0593047 micrometer/pixel
Y scale
0.0593047 micrometer/pixel
Z scale
0.5 micrometer/slice
T scale
-

Image Acquisition
Experiment type
-
Microscope type
-
Acquisition mode
-
Contrast method
-
Microscope model
-
Detector model
-
Objective model
-
Filter set
-

Summary of Methods
See details in Yoshida S, et. al. (2015) Dev Cell., 33(5):589-602.
Related paper(s)

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 )

(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.
(MeSH Terms)

Contact
Tomoya S. Kitajima , RIKEN , Center for Biosystems Dynamics Research , Laboratory for Chromosome Segregation
Contributors

OMERO Dataset
OMERO Project
Source