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The structure of TAX1BP1 UBZ1+2 provides insight into target specificity and adaptability.

Ceregido MA, Spínola Amilibia M, Buts L, Rivera-Torres J, Garcia-Pino A, Bravo J, van Nuland NA
J Mol Biol 426 674-90 (2014)
Cited: 10 times
EuropePMC logo PMID: 24239949

Abstract

TAX1BP1 is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, which is a key player in inflammatory responses, immunity and tumorigenesis. TAX1BP1 recruits A20 to the ubiquitinated signaling proteins TRAF6 and RIP1, leading to their A20-mediated deubiquitination and the disruption of IL-1-induced and TNF-induced NF-kappaB signaling, respectively. The two zinc fingers localized at its C-terminus function as novel ubiquitin-binding domains (UBZ, ubiquitin-binding zinc finger). Here we present for the first time both the solution and crystal structures of two classical UBZ domains in tandem within the human TAX1BP1. The relative orientation of the two domains is slightly different in the X-ray structure with respect to the NMR structure, indicating some degree of conformational flexibility, which is rationalized by NMR relaxation data. The observed degree of flexibility and stability between the two UBZ domains might have consequences on the recognition mechanism of interacting partners.

Reviews citing this publication (3)

  1. The exploitation of host autophagy and ubiquitin machinery by Mycobacterium tuberculosis in shaping immune responses and host defense during infection. Shariq M, Quadir N, Alam A, Zarin S, Sheikh JA, Sharma N, Samal J, Ahmad U, Kumari I, Hasnain SE, Ehtesham NZ. Autophagy 19 3-23 (2023)
  2. Multifaceted roles of TAX1BP1 in autophagy. White J, Suklabaidya S, Vo MT, Choi YB, Harhaj EW. Autophagy 19 44-53 (2023)
  3. Oligomerization of Selective Autophagy Receptors for the Targeting and Degradation of Protein Aggregates. Chen W, Shen T, Wang L, Lu K. Cells 10 1989 (2021)

Articles citing this publication (7)

  1. Dynamic post-translational modification profiling of Mycobacterium tuberculosis-infected primary macrophages. Budzik JM, Swaney DL, Jimenez-Morales D, Johnson JR, Garelis NE, Repasy T, Roberts AW, Popov LM, Parry TJ, Pratt D, Ideker T, Krogan NJ, Cox JS. Elife 9 e51461 (2020)
  2. Editorial A novel mode of ubiquitin recognition by the ubiquitin-binding zinc finger domain of WRNIP1. Suzuki N, Rohaim A, Kato R, Dikic I, Wakatsuki S, Kawasaki M. FEBS J 283 2004-2017 (2016)
  3. Structural basis for ubiquitin recognition by ubiquitin-binding zinc finger of FAAP20. Toma A, Takahashi TS, Sato Y, Yamagata A, Goto-Ito S, Nakada S, Fukuto A, Horikoshi Y, Tashiro S, Fukai S. PLoS One 10 e0120887 (2015)
  4. Ubiquitin recognition by FAAP20 expands the complex interface beyond the canonical UBZ domain. Wojtaszek JL, Wang S, Kim H, Wu Q, D'Andrea AD, Zhou P. Nucleic Acids Res 42 13997-14005 (2014)
  5. Crystallographic and modelling studies suggest that the SKICH domains from different protein families share a common Ig-like fold but harbour substantial structural variations. Yang Y, Wang G, Huang X, Du Z. J Biomol Struct Dyn 33 1385-1398 (2015)
  6. Depletion of TAX1BP1 Amplifies Innate Immune Responses during Respiratory Syncytial Virus Infection. Descamps D, Peres de Oliveira A, Gonnin L, Madrières S, Fix J, Drajac C, Marquant Q, Bouguyon E, Pietralunga V, Iha H, Morais Ventura A, Tangy F, Vidalain PO, Eléouët JF, Galloux M. J Virol 95 e0091221 (2021)
  7. On the helical arrangements of protein molecules. Dauter Z, Jaskolski M. Protein Sci 27 643-652 (2018)


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