Enhanced degradation of MDM2 by a nuclear envelope component, mouse germ cell-less

A mouse homologue of Drosophila germ cell less, mouse germ cell less-1 ( mgcl-1), encodes a nuclear envelope component essential for nuclear integrity. To analyze the molecular function of mGCL-1, we carried out two hybrid screening and found that mGCL-1 bound to the gene product of tumor susceptibi...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2003-09, Vol.308 (4), p.927-932
Main Authors: Masuhara, Masaaki, Nagao, Kenji, Nishikawa, Mitsuo, Kimura, Tohru, Nakano, Toru
Format: Article
Language:English
Subjects:
Animals
Blotting, Northern
Blotting, Western
Cell Line
Cell Nucleus - metabolism
DNA-Binding Proteins - metabolism
Endosomal Sorting Complexes Required for Transport
Humans
Luciferases - metabolism
Mice
Microscopy, Fluorescence
Nuclear Envelope - metabolism
Nuclear Proteins - metabolism
Nuclear Proteins - physiology
Plasmids - metabolism
Precipitin Tests
Protein Binding
Proto-Oncogene Proteins - metabolism
Proto-Oncogene Proteins c-mdm2
Transcription Factors - metabolism
Transcription, Genetic
Transcriptional Activation
Transfection
Tumor Cells, Cultured
Tumor Suppressor Protein p53 - metabolism
Two-Hybrid System Techniques
Ubiquitin - metabolism
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Summary:A mouse homologue of Drosophila germ cell less, mouse germ cell less-1 ( mgcl-1), encodes a nuclear envelope component essential for nuclear integrity. To analyze the molecular function of mGCL-1, we carried out two hybrid screening and found that mGCL-1 bound to the gene product of tumor susceptibility gene 101 ( tsg101). Effects of mGCL-1 on the expression of MDM2–p53 axis were examined, since TSG101 has been shown to elevate the amount of MDM2 by inhibiting the ubiquitination. mGCL-1 significantly reduced the amount of MDM2 probably by changing the sub-cellular localization of the MDM2 and facilitating the ubiquitination of MDM2. In addition, the amount of p53 was increased and transactivation by p53 was enhanced by mGCL-1. Thus, mGCL-1 turned out to be a factor modulating MDM2–p53 axis by enhanced degradation of MDM2.
ISSN:0006-291X
1090-2104
DOI:10.1016/S0006-291X(03)01497-9