Publication: Identification of lysines 36 and 37 of PARP-2 as targets for acetylation and auto-ADP-ribosylation
Identification of lysines 36 and 37 of PARP-2 as targets for acetylation and auto-ADP-ribosylation
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Haenni, S. S., Hassa, P. O., Altmeyer, M., Fey, M., Imhof, R., & Hottiger, M. O. (2008). Identification of lysines 36 and 37 of PARP-2 as targets for acetylation and auto-ADP-ribosylation. International Journal of Biochemistry & Cell Biology, 40(10), 2274–2283. https://doi.org/10.1016/j.biocel.2008.03.008
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Poly-ADP-ribose polymerase-2 (PARP-2) was described to regulate cellular functions comprising DNA surveillance, inflammation and cell differentiation by co-regulating different transcription factors. Using an in vitro and in vivo approach, we identified PARP-2 as a new substrate for the histone acetyltransferases PCAF and GCN5L. Site directed mutagenesis indicated that lysines 36 and 37, located in the nuclear localization signal of PARP-2, are the main targets for PCAF and GCN5L activity in vitro. Interestingly, acetylation of the sa
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- Haenni, S S
- Hassa, P O
- Altmeyer, M
- Fey, M
- Imhof, R
- Hottiger, M O
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Haenni, S. S., Hassa, P. O., Altmeyer, M., Fey, M., Imhof, R., & Hottiger, M. O. (2008). Identification of lysines 36 and 37 of PARP-2 as targets for acetylation and auto-ADP-ribosylation. International Journal of Biochemistry & Cell Biology, 40(10), 2274–2283. https://doi.org/10.1016/j.biocel.2008.03.008
