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LMO7 exerts an effect on mitosis progression and the spindle assembly checkpoint.
- Source :
-
The international journal of biochemistry & cell biology [Int J Biochem Cell Biol] 2018 Jan; Vol. 94, pp. 22-30. Date of Electronic Publication: 2017 Nov 20. - Publication Year :
- 2018
-
Abstract
- LMO7 (LIM domain only 7) is a transcription regulator for expression of many Emery-Dreifuss muscular dystrophy-relevant genes, and binds to α-actinin and AF6/afadin at adherens junctions for epithelial cell-cell adhesion. In this study, we found that human LMO7 interacted with the spindle assembly checkpoint (SAC) protein MAD1. LMO7 colocalized with actin filaments at the cell membrane but did not colocalize with MAD1 at kinetochores in prometaphase. Our observations reveal that overexpression but not depletion of LMO7 caused a SAC defect, and that the LIM domain of LMO7 was a determinant of its ability to interfere with kinetochore localization of the SAC proteins MAD2 and BUBR1 and cause a SAC defect though the LIM peptide itself did neither bind to MAD1, MAD2 and BUBR1 nor localize to the actin filaments. However, overexpression of LMO7 or the LIM peptide did not interfere with kinetochore localization of MAD1. Additionally, overexpression of the LIM peptide prolonged mitotic timing and interfered with chromosome congression whereas that of LMO7b did not. Taken together, we conclude that LMO7 via its LIM domain acts to control mitosis progression and exerts an effect on the SAC.<br /> (Copyright © 2017 Elsevier Ltd. All rights reserved.)
- Subjects :
- Animals
Cell Cycle Proteins chemistry
Cell Cycle Proteins genetics
Cell Line, Tumor
Humans
Interphase
Kinetochores metabolism
LIM Domain Proteins antagonists & inhibitors
LIM Domain Proteins chemistry
LIM Domain Proteins genetics
Luminescent Proteins chemistry
Luminescent Proteins genetics
Luminescent Proteins metabolism
Metaphase
Nuclear Proteins chemistry
Nuclear Proteins genetics
Peptide Fragments chemistry
Peptide Fragments genetics
Peptide Fragments metabolism
Prometaphase
Protein Domains
Protein Multimerization
Protein Transport
RNA Interference
Rats
Recombinant Fusion Proteins chemistry
Recombinant Fusion Proteins metabolism
Spindle Poles metabolism
Transcription Factors antagonists & inhibitors
Transcription Factors chemistry
Transcription Factors genetics
Actin Cytoskeleton metabolism
Cell Cycle Proteins metabolism
Cell Membrane metabolism
LIM Domain Proteins metabolism
M Phase Cell Cycle Checkpoints
Mitosis
Nuclear Proteins metabolism
Transcription Factors metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1878-5875
- Volume :
- 94
- Database :
- MEDLINE
- Journal :
- The international journal of biochemistry & cell biology
- Publication Type :
- Academic Journal
- Accession number :
- 29158164
- Full Text :
- https://doi.org/10.1016/j.biocel.2017.11.006