|
|||||
|
|
Inducible expression of catalytically active type 1 serine/threonine protein phosphatase in a human carcinoma cell line |
|
| Authors: | Jay?E?Reeder,Mark?P?Sowden,Edward?M?Messing,Peter?Klover,Emma?Villa-Moruzzi,John?W?Ludlow author-information" > author-information__contact u-icon-before" > mailto:jludlow@vestatherapeutics.com" title=" jludlow@vestatherapeutics.com" itemprop=" email" data-track=" click" data-track-action=" Email author" data-track-label=" " >Email author |
| Affiliation: | (1) Department of Pathology and Laboratory Medicine, University of Rochester School of Medicine and Dentistry, 601 Elmwood Avenue, Rochester, New York 14642, USA;(2) Department of Urology, University of Rochester School of Medicine and Dentistry, 601 Elmwood Avenue, Rochester, New York 14642, USA;(3) Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, 601 Elmwood Avenue, Rochester, New York 14642, USA;(4) University of Rochester Cancer Center, University of Rochester School of Medicine and Dentistry, 601 Elmwood Avenue, Rochester, New York 14642, USA;(5) Department of Experimental Pathology, University of Pisa, Via Roma 55, Pisa, Italy |
| Abstract: | BackgroundOne of the major cellular serine/threonine protein phosphatases is protein phosphatase type 1 (PP1). Studies employing many eukaryotic systems all point to a crucial role for PP1 activity in controlling cell cycle progression. One physiological substrate for PP1 appears to be the product of the retinoblastoma susceptibility gene (pRB), a demonstrated tumor suppressor. The growth suppressive activity of pRB is regulated by its phosphorylation state. Of critical importance is the question of the in vivo effect of PP1 activity on pRB and growth regulation. As a first step towards addressing this question, we developed an inducible PP1 expression system to investigate the regulation of PP1 activity. |
| Keywords: | |
| 本文献已被 PubMed SpringerLink 等数据库收录！ | |