DOI: 10.3724/SP.J.1206.2013.00135

Progress in Biochemistry and Biophysics (生物化学与生物物理进展) 2013/40:12 PP.1230-1238

RNF 149 Regulates The Cell Proliferation by The Polyubiquitination Mediated CD9 Degradation

Our research selected the RNF149, the novel ubiquitin ligase which owned the high identity to GRAILand belonged to the type Ⅰ transmembrane protein, as our object. By the confocal laser scanning microscope, itwas demonstrated that RNF149 is located at lysosome and the RNF149 is co-located with CD9. The interactionsbetween RNF149 and CD9 were demonstrated by immune co-precipitation.RNF149 polyubiquitinates CD9 viaubiquitin Lys-48. The HeLa cells were co-transfected with the same quantity of the CD9 plasmids and the gradientincrease quantity of the RNF149 plasmids. We found that the exogenous quantity of CD9 was decreasing with theincreased expression of the exogenous RNF149. In HEK293T cells, the knocking down RNF149 by shRNA led tothe increase of the endogenous CD9. All these evidence suggested that CD9 maybe regulated by RNF149. Inaddition, the knocking down RNF149 by shRNA led to the inhibition of the cell proliferation in HEK293T cells.This phenomenon suggested that the RNF149 possibly could be considered as the regulatory factor of the cellproliferation

Key words:RNF149,CD9,cell proliferation,ubiquitylate,ubiquitin ligase,lysosome

ReleaseDate:2015-04-18 09:14:50

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