pisco_log
banner

Functions and Mechanisms: Post-translational Modifications Mediate the Activities of DAXX

Ting Chen, Qianyin Wang, Fan Yu, Weiyang Yin, Yan Zhang*

Abstract


As a multifunctional protein, DAXX mediates apoptosis through the FAS-DAXX-ASK1-MAP2K axis. There has been a lot of research focusing on the regulation of DAXX, especially the post-translational modifications of DAXX, including ubiquitination, SUMOylation
and phosphorylation. In this paper, we summarize the functions of post-translational modifications on DAXX that have been shown to affect
DAXX's activity and stability, aiming at a better understanding of the functions of DAXX in human disease.

Keywords


DAXX; Post-translational modification; Ubiquitination; Ubiquitin-like protein modification; Phosphorylation

Full Text:

PDF

Included Database


References


[1] L.M. Rapkin, K. Ahmed, S. Dulev, R. Li, H. Kimura, A.M. Ishov, D.P. Bazett-Jones, The histone chaperone DAXX maintains the structural organization of heterochromatin domains, Epigenetics & chromatin, 8 (2015) 44.

[2] W.Y. Wani, M. Boyer-Guittaut, M. Dodson, J. Chatham, V. Darley-Usmar, J. Zhang, Regulation of autophagy by protein post-translational modification, Laboratory investigation; a journal of technical methods and pathology, 95 (2015) 14-25.

[3] Z. Lv, K.A. Rickman, L. Yuan, K. Williams, S.P. Selvam, A.N. Woosley, P.H. Howe, B. Ogretmen, A. Smogorzewska, S.K. Olsen, S.

pombe Uba1-Ubc15 Structure Reveals a Novel Regulatory Mechanism of Ubiquitin E2 Activity, Molecular cell, 65 (2017) 699-714

e696.

[4] C. Zhang, Y. Chen, X. Gan, Z. Huang, M. Zou, W. Fu, W. Xing, D. Xu, SAK-HV Decreases the Self-Ubiquitination of MEKK1 to Promote Macrophage Proliferation via MAPK/ERK and JNK Pathways, International journal of molecular sciences, 18 (2017).

[5] H. Zhang, J. He, J. Li, D. Tian, L. Gu, M. Zhou, Methylation of RASSF1A gene promoter is regulated by p53 and DAXX, FASEB J, 27

(2013) 232-242.

[6] J. Tang, T. Agrawal, Q. Cheng, L. Qu, M.D. Brewer, J. Chen, X. Yang, Phosphorylation of Daxx by ATM contributes to DNA damageinduced p53 activation, PLoS One, 8 (2013) e55813.

[7] A.V. Mendes, C.P. Grou, J.E. Azevedo, M.P. Pinto, Evaluation of the activity and substrate specificity of the human SENP family of

SUMO proteases, Biochimica et biophysica acta, 1863 (2016) 139-147.

[8] J. Salsman, L.M. Rapkin, N.N. Margam, R. Duncan, D.P. Bazett-Jones, G. Dellaire, Myogenic differentiation triggers PML nuclear body

loss and DAXX relocalization to chromocentres, Cell death & disease, 8 (2017) e2724.

[9] H.C. Lan, C.F. Wu, H.M. Shih, B.C. Chung, Death-associated protein 6 (Daxx) mediates cAMP-dependent stimulation of Cyp11a1

(P450scc) transcription, The Journal of biological chemistry, 287 (2012) 5910-5916.

[10] J.J. Song, Y.J. Lee, Tryptophan 621 and serine 667 residues of Daxx regulate its nuclear export during glucose deprivation, J Biol Chem,

279 (2004) 30573-30578.

[11] R.B. da Silva, C.R. Machado, A.R.A. Rodrigues, A.L. Pedrosa, Selective human inhibitors of ATR and ATM render Leishmania major

promastigotes sensitive to oxidative damage, PloS one, 13 (2018) e0205033.

[12] E.G. Di Domenico, E. Romano, P. Del Porto, F. Ascenzioni, Multifunctional role of ATM/Tel1 kinase in genome stability: from the DNA

damage response to telomere maintenance, BioMed research international, 2014 (2014) 787404.

[13] S.M. Ivanchuk, S. Mondal, J.T. Rutka, p14ARF interacts with DAXX: effects on HDM2 and p53, Cell Cycle, 7 (2008) 1836-1850.

[14] M. Qian, Z. Liu, L. Peng, X. Tang, F. Meng, Y. Ao, M. Zhou, M. Wang, X. Cao, B. Qin, Z. Wang, Z. Zhou, G. Wang, Z. Gao, J. Xu, B.

Liu, Boosting ATM activity alleviates aging and extends lifespan in a mouse model of progeria, eLife, 7 (2018).

[15] C.M. Hecker, M. Rabiller, K. Haglund, P. Bayer, I. Dikic, Specification of SUMO1- and SUMO2-interacting motifs, J Biol Chem, 281

(2006) 16117-16127.




DOI: http://dx.doi.org/10.70711/mhr.v3i2.9471

Refbacks

  • There are currently no refbacks.