| Literature DB >> 10100624 |
M Nanahoshi1, Y Tsujishita, C Tokunaga, S Inui, N Sakaguchi, K Hara, K Yonezawa.
Abstract
The catalytic activity of the C subunit of serine/threonine phosphatase 2A is regulated by the association with A (PR65) and B subunits. It has been reported that the alpha4 protein, a yeast homolog of the Tap42 protein, binds the C subunit of serine/threonine phosphatase 2A and protein phosphatase 2A-related protein phosphatases such as protein phosphatase 4 and protein phosphatase 6. In the present study, we showed that alpha4 binds these three phosphatases and the association of alpha4 reduces the activities of these phosphatases in vitro. In contrast, PR65 binds to the C subunit of serine/threonine phosphatase 2A but not to protein phosphatase 4 and protein phosphatase 6. These results suggest that the alpha4 protein is a common regulator of the C subunit of serine/threonine phosphatase 2A and protein phosphatase 2A-related protein phosphatases.Entities:
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Year: 1999 PMID： 10100624 DOI： 10.1016/s0014-5793(99)00189-1
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124