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Degradation of an ubiquitin‐conjugated protein is associated with myoblast differentiation in primary cell culture
Author(s) -
Gardrat Florence,
Montel Valérie,
Raymond Jacques,
Azanza JeanLouis
Publication year - 1999
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549900201413
Subject(s) - proteasome , ubiquitin , myogenesis , ubiquitin ligase , protein degradation , microbiology and biotechnology , cell fusion , ubiquitin conjugating enzyme , biology , myocyte , protein subunit , fusion protein , chemistry , biochemistry , cell , gene , recombinant dna
At the early stages of myogenesis, myoblasts fuse to form multinucleated myotubes. This morphological differentiation is the result of dynamic changes in gene regulation and expression. The ubiquitin proteasome‐dependent pathway has been reported to play an important role in many aspects of cellular functions such as regulation of growth and cell cycle progression. In this study, we showed that the amount of mRNA's corresponding to the iota subunit of the 20S proteasome, the level of the S4 subunit of the 19S complex and the 20S and 26S proteasomes peptidase activities increased during myoblast fusion. Cell permeable 20S proteasome inhibitor prevented fusion with concomitant accumulation of ubiquitin‐conjugated protein. On the other hand, inhibition of ubiquitin ligase E3 enzymes prevented the formation of ubiquitin conjugate and decreased the fusion process. These results strongly support the involvement of the ubiquitin‐proteasome proteolytic pathway in the events leading to myoblast fusion.