Association of Rpn10 with high molecular weight complex is enhanced during retinoic acid-induced differentiation of neuroblastoma cells |
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Authors: | Yoko Tayama Hiroyuki Kawahara Ryosuke Minami Masumi Shimada Hideyoshi Yokosawa |
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Institution: | (1) Department of Biochemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan |
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Abstract: | The ubiquitin-binding Rpn10 protein serves as an ubiquitin receptor that delivers client proteins to the 26S proteasome, the
protein degradation complex. It has been suggested that the ubiquitin-dependent protein degradation is critical for neuronal
differentiation and for preventing neurodegenerative diseases. Our previous study indicated the importance of Rpn10 in control
of cellular differentiation (Shimada et al., Mol Biol Cell 17:5356–5371, 2006), though the functional relevance of Rpn10 in
neuronal cell differentiation remains a mystery to be uncovered. In the present study, we have examined the level of Rpn10
in a proteasome-containing high molecular weight (HMW) protein fraction prepared from the mouse neuroblastoma cell line Neuro2a.
We here report that the protein level of Rpn10 in HMW fraction from un-differentiated Neuro2a cells was significantly lower
than that of other cultured cell lines. We have found that retinoic acid-induced neural differentiation of Neuro2a cells significantly
stimulates the incorporation of Rpn10 into HMW fractions, although the amounts of 26S proteasome subunits were not changed.
Our findings provide the first evidence that the modulation of Rpn10 is linked to the control of retinoic acid-induced differentiation
of neuroblastoma cells. |
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Keywords: | Rpn10 Ubiquitin 26S proteasome Retinoic acid Neuron |
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