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Zhou J Wan B Li R Gu X Zhong Z Wang Y Yu L 《Biochemical and biophysical research communications》2012,422(4):647-652
Brain-specific kinase 2 (BRSK2) was classified as an AMP-activated protein kinase (AMPK)-related kinase and one of the substrates of LKB1. Studies on homologs of BRSK2 in mice, SADA and SADB, implied that it might be involved in the regulation of cell polarity and cell cycle. However, physiological functions and molecular regulatory mechanisms of BRSK2 are incompletely understood. In this study, we isolated a novel BRSK2-interacting protein, c-Jun activation domain-binding protein-1 (Jab1), which was reported to mediate degradation of multiple proteins and positively regulate cell cycle progression. GST pull-down and immunoprecipitation assays revealed the direct interaction between BRSK2 and Jab1 in vitro and in vivo, respectively. The co-localization between Jab1 and BRSK2 in the perinuclear region was observed. Intriguingly, Jab1 promoted the ubiquitination and proteasome-dependent degradation of BRSK2. Silencing of endogenous Jab1 increased the cellular BRSK2 protein level. Consistent with this, BRSK2-mediated cell cycle arrest at the G2/M phase in mammalian cells was reversed by exogenous Jab1. Taken together, our findings provide a novel regulatory mechanism of BRSK2 through direct interaction with Jab1. 相似文献
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An N-Terminal Dimerization Domain Permits Homeodomain Proteins To Choose Compatible Partners and Initiate Sexual Development in the Mushroom Coprinus cinereus 总被引:1,自引:0,他引:1 下载免费PDF全文
Banham AH Asante-Owusu RN Gottgens B Thompson S Kingsnorth CS Mellor E Casselton LA 《The Plant cell》1995,7(6):773-783
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