| pubmed-article:17374606 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17374606 | lifeskim:mentions | umls-concept:C0006104 | lld:lifeskim |
| pubmed-article:17374606 | lifeskim:mentions | umls-concept:C1517080 | lld:lifeskim |
| pubmed-article:17374606 | lifeskim:mentions | umls-concept:C0040648 | lld:lifeskim |
| pubmed-article:17374606 | lifeskim:mentions | umls-concept:C1956003 | lld:lifeskim |
| pubmed-article:17374606 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:17374606 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
| pubmed-article:17374606 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:17374606 | pubmed:dateCreated | 2007-5-7 | lld:pubmed |
| pubmed-article:17374606 | pubmed:abstractText | Pax-6 is an evolutionarily conserved transcription factor and acts high up in the regulatory hierarchy controlling eye and brain development in humans, mice, zebrafish, and Drosophila. Previous studies have shown that Pax-6 is a phosphoprotein, and its phosphorylation by ERK, p38, and homeodomain-interacting protein kinase 2 greatly enhances its transactivation activity. However, the protein phosphatases responsible for the dephosphorylation of Pax-6 remain unknown. Here, we present both in vitro and in vivo evidence to show that protein serine/threonine phosphatase-1 is a major phosphatase that directly dephosphorylates Pax-6. First, purified protein phosphatase-1 directly dephosphorylates Pax-6 in vitro. Second, immunoprecipitation-linked Western blot revealed that both protein phosphatase-1alpha and protein phosphatase-1beta interact with Pax-6. Third, overexpression of protein phosphatase-1 in human lens epithelial cells leads to dephosphorylation of Pax-6. Finally, inhibition of protein phosphatase-1 activity by calyculin A or knockdown of protein phosphatase-1alpha and protein phosphatase-1beta by RNA interference leads to enhanced phosphorylation of Pax-6. Moreover, our results also demonstrate that dephosphorylation of Pax-6 by protein phosphatase-1 significantly modulates its function in regulating expression of both exogenous and endogenous genes. These results demonstrate that protein phosphatase 1 acts as a major phosphatase to dephosphorylate Pax-6 and modulate its function. | lld:pubmed |
| pubmed-article:17374606 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17374606 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17374606 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17374606 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17374606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17374606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17374606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17374606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17374606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17374606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17374606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17374606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17374606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17374606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17374606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17374606 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17374606 | pubmed:month | May | lld:pubmed |
| pubmed-article:17374606 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:17374606 | pubmed:author | pubmed-author:LeiX HXH | lld:pubmed |
| pubmed-article:17374606 | pubmed:author | pubmed-author:FarrR KRK | lld:pubmed |
| pubmed-article:17374606 | pubmed:author | pubmed-author:LiYongY | lld:pubmed |
| pubmed-article:17374606 | pubmed:author | pubmed-author:LiuYanY | lld:pubmed |
| pubmed-article:17374606 | pubmed:author | pubmed-author:ZhangLanL | lld:pubmed |
| pubmed-article:17374606 | pubmed:author | pubmed-author:ChenLiliL | lld:pubmed |
| pubmed-article:17374606 | pubmed:author | pubmed-author:LiuYunY | lld:pubmed |
| pubmed-article:17374606 | pubmed:author | pubmed-author:FengHaoH | lld:pubmed |
| pubmed-article:17374606 | pubmed:author | pubmed-author:HuangXiaoqinX | lld:pubmed |
| pubmed-article:17374606 | pubmed:author | pubmed-author:LiuJinpingJ | lld:pubmed |
| pubmed-article:17374606 | pubmed:author | pubmed-author:QinJichaoJ | lld:pubmed |
| pubmed-article:17374606 | pubmed:author | pubmed-author:LiuWen-BinWB | lld:pubmed |
| pubmed-article:17374606 | pubmed:author | pubmed-author:GongLiliL | lld:pubmed |
| pubmed-article:17374606 | pubmed:author | pubmed-author:SunShumingS | lld:pubmed |
| pubmed-article:17374606 | pubmed:author | pubmed-author:ChenHe-GeHG | lld:pubmed |
| pubmed-article:17374606 | pubmed:author | pubmed-author:XiaoYameiY | lld:pubmed |
| pubmed-article:17374606 | pubmed:author | pubmed-author:LiDavid W-CDW | lld:pubmed |
| pubmed-article:17374606 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17374606 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:17374606 | pubmed:volume | 282 | lld:pubmed |
| pubmed-article:17374606 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17374606 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17374606 | pubmed:pagination | 13954-65 | lld:pubmed |
| pubmed-article:17374606 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:17374606 | pubmed:meshHeading | pubmed-meshheading:17374606... | lld:pubmed |
| pubmed-article:17374606 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17374606 | pubmed:articleTitle | Protein phosphatase-1 modulates the function of Pax-6, a transcription factor controlling brain and eye development. | lld:pubmed |
| pubmed-article:17374606 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE 68198, USA. | lld:pubmed |
| pubmed-article:17374606 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17374606 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17374606 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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