作者: Arianna Ferro , Felice Amato , Patrizia Rubino , Davide Randazzo , Thorsten Wolff
DOI: 10.1016/J.BBAMCR.2007.09.002
关键词:
摘要: Alpha-enolase is a key glycolytic enzyme that plays functional role in several physiological processes depending on the cellular localization. The mainly localized cytoplasm whereas an alternative translated form, named MBP-1, predominantly nuclear. MBP-1 protein has been characterized as c-Myc promoter binding negatively controls transcription. In present study, we identified kelch NS1-BP one of alpha-enolase/MBP-1 partners by using yeast two-hybrid screening. Although originally described nucleus, provide evidence also interacts with actin human cells, reported for most kelch-containing proteins. Here showed alpha-enolase and associate vitro vivo GST pull-down assays coimmunoprecipitation experiments; subsequent immunofluorescent staining confirmed colocalization proteins within cells. Furthermore, analyses performed cotransfection revealed enhances inhibitory effect exerted promoter. mammalian overexpression both resulted increased repression basal transcription consistently affected steady state levels endogenous mRNA. These findings further support distinct roles its variant maintaining cell homeostasis. Moreover, our data suggest novel function control proliferation.