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Characterization of Aes nuclear foci in colorectal cancer cells.
- Source :
-
Journal of biochemistry [J Biochem] 2016 Jan; Vol. 159 (1), pp. 133-40. Date of Electronic Publication: 2015 Jul 29. - Publication Year :
- 2016
-
Abstract
- Amino-terminal enhancer of split (Aes) is a member of Groucho/Transducin-like enhancer (TLE) family. Aes is a recently found metastasis suppressor of colorectal cancer (CRC) that inhibits Notch signalling, and forms nuclear foci together with TLE1. Although some Notch-associated proteins are known to form subnuclear bodies, little is known regarding the dynamics or functions of these structures. Here, we show that Aes nuclear foci in CRC observed under an electron microscope are in a rather amorphous structure, lacking surrounding membrane. Investigation of their behaviour during the cell cycle by time-lapse cinematography showed that Aes nuclear foci dissolve during mitosis and reassemble after completion of cytokinesis. We have also found that heat shock cognate 70 (HSC70) is an essential component of Aes foci. Pharmacological inhibition of the HSC70 ATPase activity with VER155008 reduces Aes focus formation. These results provide insight into the understanding of Aes-mediated inhibition of Notch signalling.<br /> (© The Authors 2015. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.)
- Subjects :
- Adenosine Triphosphatases antagonists & inhibitors
Animals
Cell Nucleus ultrastructure
Co-Repressor Proteins
Cytokinesis
HCT116 Cells
HEK293 Cells
HSC70 Heat-Shock Proteins antagonists & inhibitors
Humans
Mice
Mice, Inbred C57BL
Microscopy, Fluorescence
Microscopy, Immunoelectron
Mitosis
Purine Nucleosides pharmacology
Receptors, Notch metabolism
Repressor Proteins genetics
Signal Transduction
Time-Lapse Imaging
Adenosine Triphosphatases metabolism
Cell Nucleus metabolism
Colorectal Neoplasms metabolism
HSC70 Heat-Shock Proteins metabolism
Repressor Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1756-2651
- Volume :
- 159
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Journal of biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 26229111
- Full Text :
- https://doi.org/10.1093/jb/mvv077