The p53-targeting human phosphatase hCdc14A interacts with the Cdk1/cyclin B complex and is differentially expressed in human cancers
<p>Abstract</p> <p>Background</p> <p>The evolutionary conserved cyclin-dependent kinase phosphatase hCdc14A has been shown to play potential roles in the regulation of mitotic exit and in the centrosome duplication cycle. We have recently shown that hCdc14A also can int...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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BMC
2006-06-01
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| Series: | Molecular Cancer |
| Online Access: | http://www.molecular-cancer.com/content/5/1/25 |
| _version_ | 1811252014868332544 |
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| author | Li Liwu Dixon Jack E Hanasoge Sheela Derheimer Frederick A Starks Adrienne M Paulsen Michelle T Ljungman Mats |
| author_facet | Li Liwu Dixon Jack E Hanasoge Sheela Derheimer Frederick A Starks Adrienne M Paulsen Michelle T Ljungman Mats |
| author_sort | Li Liwu |
| collection | DOAJ |
| description | <p>Abstract</p> <p>Background</p> <p>The evolutionary conserved cyclin-dependent kinase phosphatase hCdc14A has been shown to play potential roles in the regulation of mitotic exit and in the centrosome duplication cycle. We have recently shown that hCdc14A also can interact with the tumor suppressor p53 both <it>in vitro </it>and <it>in vivo </it>and specifically dephosphorylates the ser315 site of p53 <it>in vitro</it>. In this study we developed antibodies against hCdc14A to investigate the expression and regulation of hCdc14A in human tissues and cancer cells.</p> <p>Results</p> <p>We show that hCdc14A is differentially expressed in human tissues and in 75 cancer cell lines examined. Treatments with the histone deacetylase inhibitor TSA, the demethylating agent 5-aza-2'-deoxycytodine or the proteasome inhibitor MG132 significantly induced expression of hCdc14A in cell lines expressing low or undetectable levels of hCdc14A. There was a strong bias for low expression of hCdc14A in cancer cell lines harboring wild-type p53, suggesting that high Cdc14A expression is not compatible with wild-type p53 expression. We present evidence for a role for hCdc14A in the dephosphorylation of the ser315 site of p53 <it>in vivo </it>and that hCdc14A forms a complex with Cdk1/cyclin B during interphase but not during mitosis.</p> <p>Conclusion</p> <p>Our results that hCdc14A is differentially expressed in human cancer cells and that hCdc14A can interact with both p53 and the Cdk1/cyclin B complex may implicate that dysregulation of hCdc14A expression may play a role in carcinogenesis.</p> |
| first_indexed | 2024-04-12T16:28:32Z |
| format | Article |
| id | doaj.art-a54169db4a9e41d0b51fdb22841800fc |
| institution | Directory Open Access Journal |
| issn | 1476-4598 |
| language | English |
| last_indexed | 2024-04-12T16:28:32Z |
| publishDate | 2006-06-01 |
| publisher | BMC |
| record_format | Article |
| series | Molecular Cancer |
| spelling | doaj.art-a54169db4a9e41d0b51fdb22841800fc2022-12-22T03:25:16ZengBMCMolecular Cancer1476-45982006-06-01512510.1186/1476-4598-5-25The p53-targeting human phosphatase hCdc14A interacts with the Cdk1/cyclin B complex and is differentially expressed in human cancersLi LiwuDixon Jack EHanasoge SheelaDerheimer Frederick AStarks Adrienne MPaulsen Michelle TLjungman Mats<p>Abstract</p> <p>Background</p> <p>The evolutionary conserved cyclin-dependent kinase phosphatase hCdc14A has been shown to play potential roles in the regulation of mitotic exit and in the centrosome duplication cycle. We have recently shown that hCdc14A also can interact with the tumor suppressor p53 both <it>in vitro </it>and <it>in vivo </it>and specifically dephosphorylates the ser315 site of p53 <it>in vitro</it>. In this study we developed antibodies against hCdc14A to investigate the expression and regulation of hCdc14A in human tissues and cancer cells.</p> <p>Results</p> <p>We show that hCdc14A is differentially expressed in human tissues and in 75 cancer cell lines examined. Treatments with the histone deacetylase inhibitor TSA, the demethylating agent 5-aza-2'-deoxycytodine or the proteasome inhibitor MG132 significantly induced expression of hCdc14A in cell lines expressing low or undetectable levels of hCdc14A. There was a strong bias for low expression of hCdc14A in cancer cell lines harboring wild-type p53, suggesting that high Cdc14A expression is not compatible with wild-type p53 expression. We present evidence for a role for hCdc14A in the dephosphorylation of the ser315 site of p53 <it>in vivo </it>and that hCdc14A forms a complex with Cdk1/cyclin B during interphase but not during mitosis.</p> <p>Conclusion</p> <p>Our results that hCdc14A is differentially expressed in human cancer cells and that hCdc14A can interact with both p53 and the Cdk1/cyclin B complex may implicate that dysregulation of hCdc14A expression may play a role in carcinogenesis.</p>http://www.molecular-cancer.com/content/5/1/25 |
| spellingShingle | Li Liwu Dixon Jack E Hanasoge Sheela Derheimer Frederick A Starks Adrienne M Paulsen Michelle T Ljungman Mats The p53-targeting human phosphatase hCdc14A interacts with the Cdk1/cyclin B complex and is differentially expressed in human cancers Molecular Cancer |
| title | The p53-targeting human phosphatase hCdc14A interacts with the Cdk1/cyclin B complex and is differentially expressed in human cancers |
| title_full | The p53-targeting human phosphatase hCdc14A interacts with the Cdk1/cyclin B complex and is differentially expressed in human cancers |
| title_fullStr | The p53-targeting human phosphatase hCdc14A interacts with the Cdk1/cyclin B complex and is differentially expressed in human cancers |
| title_full_unstemmed | The p53-targeting human phosphatase hCdc14A interacts with the Cdk1/cyclin B complex and is differentially expressed in human cancers |
| title_short | The p53-targeting human phosphatase hCdc14A interacts with the Cdk1/cyclin B complex and is differentially expressed in human cancers |
| title_sort | p53 targeting human phosphatase hcdc14a interacts with the cdk1 cyclin b complex and is differentially expressed in human cancers |
| url | http://www.molecular-cancer.com/content/5/1/25 |
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