CCDC134 interacts with hADA2a and functions as a regulator of hADA2a in acetyltransferase activity, DNA damage-induced apoptosis and cell cycle arrest
作者： Jing Huang , Li Zhang , Wei Liu , Qinyuan Liao , Taiping Shi
DOI: 10.1007/S00418-012-0932-5
关键词:
摘要: Human transcriptional adaptor hADA2a is an important component of the general control nonderepressible 5 (GCN5) histone acetyltransferase complex. Here, we report that coiled-coil domain containing 134 (CCDC134), a novel nuclear protein, binds to and enhances stability protein in unstressed conditions. Furthermore, CCDC134 was found participate p300/CBP-associated factor (PCAF) complex via affect activity We also increased PCAF-dependent K320 acetylation p53 presence overexpression. Moreover, demonstrated biological significance interaction between hADA2a. showed obvious accumulation after ultraviolet (UV) irradiation, knockdown endogenous suppressed hADA2a-induced cell apoptosis G1/S cycle arrest. Together, our findings indicate might act as regulator hADA2a, plays roles PCAF its UV-induced DNA damage repair.
springer.com
core.ac.uk 
sci-hub.se 参考文章(34)
CA Dinarello, Biologic basis for interleukin-1 in disease Blood. ,vol. 87, pp. 2095- 2147 ,(1996) , 10.1182/BLOOD.V87.6.2095.BLOODJOURNAL8762095
M Perry, R Chalkley, Histone acetylation increases the solubility of chromatin and occurs sequentially over most of the chromatin. A novel model for the biological role of histone acetylation. Journal of Biological Chemistry. ,vol. 257, pp. 7336- 7347 ,(1982) , 10.1016/S0021-9258(18)34382-5
Marjorie Brand, Ken Yamamoto, Adrien Staub, Laszlo Tora, Identification of TATA-binding Protein-free TAFII-containing Complex Subunits Suggests a Role in Nucleosome Acetylation and Signal Transduction Journal of Biological Chemistry. ,vol. 274, pp. 18285- 18289 ,(1999) , 10.1074/JBC.274.26.18285
Susanne Müller, Paola Scaffidi, Bernard Degryse, Tiziana Bonaldi, Lorenza Ronfani, Alessandra Agresti, Monica Beltrame, Marco E Bianchi, The double life of HMGB1 chromatin protein: architectural factor and extracellular signal The EMBO Journal. ,vol. 20, pp. 4337- 4340 ,(2001) , 10.1093/EMBOJ/20.16.4337
K. Sakaguchi, J. E. Herrera, S.'i. Saito, T. Miki, M. Bustin, A. Vassilev, C. W. Anderson, E. Appella, DNA damage activates p53 through a phosphorylation–acetylation cascade Genes & Development. ,vol. 12, pp. 2831- 2841 ,(1998) , 10.1101/GAD.12.18.2831
J. Huang, T. Shi, T. Ma, Y. Zhang, X. Ma, Y. Lu, Q. Song, W. Liu, D. Ma, X. Qiu, CCDC134, a novel secretory protein, inhibits activation of ERK and JNK, but not p38 MAPK Cellular and Molecular Life Sciences. ,vol. 65, pp. 338- 349 ,(2008) , 10.1007/S00018-007-7448-5
Tetsuya Ueda, Michiteru Yoshida, HMGB proteins and transcriptional regulation Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms. ,vol. 1799, pp. 114- 118 ,(2010) , 10.1016/J.BBAGRM.2009.11.005
Vasily V Ogryzko, Tomohiro Kotani, Xiaolong Zhang, R.Louis Schiltz, Tazuko Howard, Xiang-Jiao Yang, Bruce H Howard, Jun Qin, Yoshihiro Nakatani, Histone-like TAFs within the PCAF Histone Acetylase Complex Cell. ,vol. 94, pp. 35- 44 ,(1998) , 10.1016/S0092-8674(00)81219-2
Wafik S El-Deiry, Takashi Tokino, Victor E Velculescu, Daniel B Levy, Ramon Parsons, Jeffrey M Trent, David Lin, W Edward Mercer, Kenneth W Kinzler, Bert Vogelstein, WAF1, a potential mediator of p53 tumor suppression Cell. ,vol. 75, pp. 817- 825 ,(1993) , 10.1016/0092-8674(93)90500-P
Miroslava Buryskova, Martin Pospisek, Arnhild Grothey, Thomas Simmet, Ladislav Burysek, Intracellular Interleukin-1α Functionally Interacts with Histone Acetyltransferase Complexes Journal of Biological Chemistry. ,vol. 279, pp. 4017- 4026 ,(2004) , 10.1074/JBC.M306342200