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Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C.

Escobar-Cabrera E, Lau DK, Giovinazzi S, Ishov AM, McIntosh LP
Structure 18 1642-53 (2010)
Cited: 23 times
EuropePMC logo PMID: 21134643

Abstract

DAXX is a scaffold protein with diverse roles including transcription and cell cycle regulation. Using NMR spectroscopy, we demonstrate that the C-terminal half of DAXX is intrinsically disordered, whereas a folded domain is present near its N terminus. This domain forms a left-handed four-helix bundle (H1, H2, H4, H5). However, due to a crossover helix (H3), this topology differs from that of the Sin3 PAH domain, which to date has been used as a model for DAXX. The N-terminal residues of the tumor suppressor Rassf1C fold into an amphipathic α helix upon binding this DAXX domain via a shallow cleft along the flexible helices H2 and H5 (K(D) ∼60 μM). Based on a proposed DAXX recognition motif as hydrophobic residues preceded by negatively charged groups, we found that peptide models of p53 and Mdm2 also bound the helical bundle. These data provide a structural foundation for understanding the diverse functions of DAXX.

Articles - 2kzu mentioned but not cited (4)

  1. Modeling of RAS complexes supports roles in cancer for less studied partners. Engin HB, Carlin D, Pratt D, Carter H. BMC Biophys 10 5 (2017)
  2. Letter Structural basis for DAXX interaction with ATRX. Wang X, Zhao Y, Zhang J, Chen Y. Protein Cell 8 767-771 (2017)
  3. The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins. Chakraborty S, Rendón-Ramírez A, Ásgeirsson B, Dutta M, Ghosh AS, Oda M, Venkatramani R, Rao BJ, Dandekar AM, Goñi FM. F1000Res 2 286 (2013)
  4. Stitched peptides as potential cell permeable inhibitors of oncogenic DAXX protein. Jelinska C, Kannan S, Frosi Y, Ramlan SR, Winnerdy F, Lakshminarayanan R, Johannes CW, Brown CJ, Phan AT, Rhodes D, Verma CS. RSC Chem Biol 4 1096-1110 (2023)


Reviews citing this publication (4)

  1. RASSF tumor suppressor gene family: biological functions and regulation. Volodko N, Gordon M, Salla M, Ghazaleh HA, Baksh S. FEBS Lett 588 2671-2684 (2014)
  2. DAXX in cancer: phenomena, processes, mechanisms and regulation. Mahmud I, Liao D. Nucleic Acids Res 47 7734-7752 (2019)
  3. DAXX Is a Crucial Factor for Proper Development of Mammalian Oocytes and Early Embryos. Bogolyubova I, Bogolyubov D. Int J Mol Sci 22 1313 (2021)
  4. Dynamic Activity of Histone H3-Specific Chaperone Complexes in Oncogenesis. Wen T, Chen QY. Front Oncol 11 806974 (2021)

Articles citing this publication (15)

  1. Cancer Mutations of the Tumor Suppressor SPOP Disrupt the Formation of Active, Phase-Separated Compartments. Bouchard JJ, Otero JH, Scott DC, Szulc E, Martin EW, Sabri N, Granata D, Marzahn MR, Lindorff-Larsen K, Salvatella X, Schulman BA, Mittag T. Mol Cell 72 19-36.e8 (2018)
  2. p53 SUMOylation promotes its nuclear export by facilitating its release from the nuclear export receptor CRM1. Santiago A, Li D, Zhao LY, Godsey A, Liao D. Mol Biol Cell 24 2739-2752 (2013)
  3. Structural and mechanistic insights into ATRX-dependent and -independent functions of the histone chaperone DAXX. Hoelper D, Huang H, Jain AY, Patel DJ, Lewis PW. Nat Commun 8 1193 (2017)
  4. Retroviral DNA methylation and epigenetic repression are mediated by the antiviral host protein Daxx. Shalginskikh N, Poleshko A, Skalka AM, Katz RA. J Virol 87 2137-2150 (2013)
  5. Characterizing the N- and C-terminal Small ubiquitin-like modifier (SUMO)-interacting motifs of the scaffold protein DAXX. Escobar-Cabrera E, Okon M, Lau DK, Dart CF, Bonvin AM, McIntosh LP. J Biol Chem 286 19816-19829 (2011)
  6. DAXX co-folds with H3.3/H4 using high local stability conferred by the H3.3 variant recognition residues. DeNizio JE, Elsässer SJ, Black BE. Nucleic Acids Res 42 4318-4331 (2014)
  7. DNA damage-induced regulatory interplay between DAXX, p53, ATM kinase and Wip1 phosphatase. Brazina J, Svadlenka J, Macurek L, Andera L, Hodny Z, Bartek J, Hanzlikova H. Cell Cycle 14 375-387 (2015)
  8. Regulation of mitosis and taxane response by Daxx and Rassf1. Giovinazzi S, Lindsay CR, Morozov VM, Escobar-Cabrera E, Summers MK, Han HS, McIntosh LP, Ishov AM. Oncogene 31 13-26 (2012)
  9. RASSF Signalling and DNA Damage: Monitoring the Integrity of the Genome? Scrace SF, O'Neill E. Mol Biol Int 2012 141732 (2012)
  10. Phosphorylation drives an apoptotic protein to activate antiapoptotic genes: paradigm of influenza A matrix 1 protein function. Halder UC, Bhowmick R, Roy Mukherjee T, Nayak MK, Chawla-Sarkar M. J Biol Chem 288 14554-14568 (2013)
  11. Performance of DAXX Immunohistochemistry as a Screen for DAXX Mutations in Pancreatic Neuroendocrine Tumors. Hechtman JF, Klimstra DS, Nanjangud G, Frosina D, Shia J, Jungbluth AA. Pancreas 48 396-399 (2019)
  12. Tumor suppressor functions of DAXX through histone H3.3/H3K9me3 pathway in pancreatic NETs. Ueda H, Akiyama Y, Shimada S, Mogushi K, Serizawa M, Matsumura S, Mitsunori Y, Aihara A, Ban D, Ochiai T, Kudo A, Tanabe M, Tanaka S. Endocr Relat Cancer 25 619-631 (2018)
  13. Letter Structural and biochemical characterization of DAXX-ATRX interaction. Li Z, Zhao D, Xiang B, Li H. Protein Cell 8 762-766 (2017)
  14. Multifunctional adaptor protein Daxx interacts with chromatin-remodelling ATPase Brg1. Svadlenka J, Brazina J, Hanzlikova H, Cermak L, Andera L. Biochem Biophys Rep 5 246-252 (2016)
  15. DAXX drives de novo lipogenesis and contributes to tumorigenesis. Mahmud I, Tian G, Wang J, Hutchinson TE, Kim BJ, Awasthee N, Hale S, Meng C, Moore A, Zhao L, Lewis JE, Waddell A, Wu S, Steger JM, Lydon ML, Chait A, Zhao LY, Ding H, Li JL, Purayil HT, Huo Z, Daaka Y, Garrett TJ, Liao D. Nat Commun 14 1927 (2023)


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