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Proliferating cell nuclear antigen destabilizes c-Abl tyrosine kinase and regulates cell apoptosis in response to DNA damage.
- Source :
- Apoptosis; Mar2009, Vol. 14 Issue 3, p268-275, 8p, 3 Diagrams, 1 Graph
- Publication Year :
- 2009
-
Abstract
- The tyrosine kinase, c-Abl, plays important roles in many aspects of cellular function. The activity of c-Abl is tightly controlled, but the underlying mechanism is unclear. Recent studies suggest that c-Abl function is regulated by distinct lipids in different cell types. In the present study, we show that the DNA replication factor, proliferating cell nuclear antigen (PCNA), interacts with c-Abl and destabilizes c-Abl by promoting its polyubiquitination and degradation. Moreover, deletion of a domain in c-Abl, the PIP box, disrupts its interaction with PCNA, abolishes the PCNA-induced degradation of nuclear c-Abl, and substantially increases the nuclear c-Abl apoptotic function. These findings indicate that PCNA negatively regulates the stability of c-Abl and thereby inhibits apoptosis in the response to DNA damage. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 13608185
- Volume :
- 14
- Issue :
- 3
- Database :
- Complementary Index
- Journal :
- Apoptosis
- Publication Type :
- Academic Journal
- Accession number :
- 36548660
- Full Text :
- https://doi.org/10.1007/s10495-009-0313-2