2024

Vringer, E. et al. (2024) Mitochondrial outer membrane integrity regulates a ubiquitin-dependent and NF-κB-mediated inflammatory response. EMBO Journal, 43(6), pp. 904-930. (doi: 10.1038/s44318-024-00044-1) (PMID:38337057) (PMCID:PMC10943237)

2023

Nikolatou, K. et al. (2023) PTEN deficiency exposes a requirement for an ARF GTPase module for integrin-dependent invasion in ovarian cancer. EMBO Journal, 42, e1139. (doi: 10.15252/embj.2023113987) (PMID:37577760) (PMCID:PMC10505920)

Villar, V. H. et al. (2023) Hepatic glutamine synthetase controls N5-methylglutamine in homeostasis and cancer. Nature Chemical Biology, 19(3), pp. 292-300. (doi: 10.1038/s41589-022-01154-9) (PMID:36280791) (PMCID:PMC9974483)

Schmidt, T. et al. (2023) eIF4A1-dependent mRNAs employ purine-rich 5’UTR sequences to activate localised eIF4A1-unwinding through eIF4A1-multimerisation to facilitate translation. Nucleic Acids Research, 51(4), pp. 1859-1879. (doi: 10.1093/nar/gkad030) (PMID:36727461) (PMCID:PMC9976904)

Chen, H. et al. (2023) PRL2 phosphatase enhances oncogenic FLT3 signaling via dephosphorylation of the E3 ubiquitin ligase CBL at tyrosine 371. Blood Vessels, 141(3), pp. 244-259. (doi: 10.1182/blood.2022016580) (PMID:36206490)

2022

Kowalczyk, D., Nakasone, M. A., Smith, B. O. and Huang, D. T. (2022) Bivalent binding of p14ARF to MDM2 RING and acidic domains inhibits E3 ligase function. Life Science Alliance, 5(12), e202201472. (doi: 10.26508/lsa.202201472) (PMID:35944929) (PMCID:PMC9366199)

Nakasone, M. A., Majorek, K. A., Gabrielsen, M. , Sibbet, G. J., Smith, B. O. and Huang, D. T. (2022) Structure of UBE2K-Ub/E3/polyUb reveals mechanisms of K48-linked Ub chain extension. Nature Chemical Biology, 18, pp. 422-431. (doi: 10.1038/s41589-021-00952-x) (PMID:35027744) (PMCID:PMC8964413)

2021

Ahmed, S. F., Buetow, L., Gabrielsen, M. , Lilla, S., Sibbet, G. J., Sumpton, D., Zanivan, S. , Hedley, A., Clark, W. and Huang, D. T. (2021) E3 ligase-inactivation rewires CBL interactome to elicit oncogenesis by hijacking RTK–CBL–CIN85 axis. Oncogene, 40(12), pp. 2149-2164. (doi: 10.1038/s41388-021-01684-x) (PMID:33627783) (PMCID:PMC7994203)

Magnussen, H. M. and Huang, D. T. (2021) Identification of a catalytic active but non-aggregating MDM2 RING domain variant. Journal of Molecular Biology, 433(5), 166807. (doi: 10.1016/j.jmb.2021.166807) (PMID:33450248) (PMCID:PMC7895813)

Humpton, T. J. et al. (2021) Differential requirements for MDM2 E3 activity during embryogenesis and in adult mice. Genes and Development, 35(1-2), pp. 117-132. (doi: 10.1101/gad.341875.120) (PMID:33334825) (PMCID:PMC7778261)

2020

Chatrin, C., Gabrielsen, M. , Buetow, L., Nakasone, M. A., Ahmed, S. F., Sumpton, D., Sibbet, G. J., Smith, B. O. and Huang, D. T. (2020) Structural insights into ADP-ribosylation of ubiquitin by Deltex family E3 ubiquitin ligases. Science Advances, 6(38), eabc0418. (doi: 10.1126/sciadv.abc0418) (PMID:32948590) (PMCID:PMC7500938)

Ahmed, S. F., Buetow, L., Gabrielsen, M. , Lilla, S., Chatrin, C., Sibbet, G. J., Zanivan, S. and Huang, D. T. (2020) DELTEX2 C-terminal domain recognizes and recruits ADP-ribosylated proteins for ubiquitination. Science Advances, 6(34), eabc0629. (doi: 10.1126/sciadv.abc0629) (PMID:32937373) (PMCID:PMC7442474)

Magnussen, H. M. et al. (2020) Structural basis for DNA damage-induced phosphoregulation of MDM2 RING domain. Nature Communications, 11, 2094. (doi: 10.1038/s41467-020-15783-y) (PMID:32350255) (PMCID:PMC7190642)

2019

Gabrielsen, M., Buetow, L., Kowalczyk, D., Zhang, W., Sidhu, S. S. and Huang, D. T. (2019) Identification and characterization of mutations in ubiquitin required for non-covalent dimer formation. Structure, 27(9), 1452-1459.e4. (doi: 10.1016/j.str.2019.06.008) (PMID:31303481) (PMCID:PMC6720194)

Patel, A., Sibbet, G. J. and Huang, D. T. (2019) Structural insights into non-covalent ubiquitin activation of the cIAP1-UbcH5B~ubiquitin complex. Journal of Biological Chemistry, 294, pp. 1240-1249. (doi: 10.1074/jbc.RA118.006045) (PMID:30523153) (PMCID:PMC6349121)

2018

Buetow, L., Gabrielsen, M. and Huang, D. (2018) Single-Turnover RING/U-Box E3-Mediated Lysine Discharge Assays. In: Mayor, T. and Kleiger, G. (eds.) The Ubiquitin Proteasome System. Series: Methods in Molecular Biology (1844). Humana Press, pp. 19-31. ISBN 9781493987054 (doi: 10.1007/978-1-4939-8706-1_2)

Marciano, G., Da Vela, S., Tria, G., Svergun, D. I., Byron, O. and Huang, D. T. (2018) Structure specific recognition protein-1 (SSRP1) is an elongated homodimer that binds histones. Journal of Biological Chemistry, 293(26), pp. 10071-10083. (doi: 10.1074/jbc.RA117.000994) (PMID:29764934) (PMCID:PMC6028955)

2017

Gabrielsen, M. , Buetow, L., Nakasone, M. A., Ahmed, S. F., Sibbet, G. J., Smith, B. O. , Zhang, W., Sidhu, S. S. and Huang, D. T. (2017) A general strategy for discovery of inhibitors and activators of RING and U-box E3 ligases with ubiquitin variants. Molecular Cell, 68(2), 456-470.e10. (doi: 10.1016/j.molcel.2017.09.027) (PMID:29053960) (PMCID:PMC5655547)

Nomura, K. , Klejnot, M., Kowalczyk, D., Hock, A. K., Sibbet, G. J., Vousden, K. and Huang, D. T. (2017) Structural analysis of MDM2 RING separates degradation from regulation of p53 transcription activity. Nature Structural and Molecular Biology, 24(7), pp. 578-587. (doi: 10.1038/nsmb.3414) (PMID:28553961)

2016

Buetow, L. and Huang, D. T. (2016) Structural insights into the catalysis and regulation of E3 ubiquitin ligases. Nature Reviews Molecular Cell Biology, 17(10), pp. 626-642. (doi: 10.1038/nrm.2016.91) (PMID:27485899)

Buetow, L., Tria, G., Ahmed, S. F., Hock, A., Dou, H., Sibbet, G. J., Svergun, D. I. and Huang, D. T. (2016) Casitas B-lineage lymphoma linker helix mutations found in myeloproliferative neoplasms affect conformation. BMC Biology, 14, 76. (doi: 10.1186/s12915-016-0298-6) (PMID:27609087) (PMCID:PMC5015263)

Marciano, G. and Huang, D.T. (2016) Structure of the human histone chaperone FACT Spt16 N-terminal domain. Acta Crystallographica. Section F: Structural Biology Communications, 72(2), pp. 121-128. (doi: 10.1107/s2053230x15024565) (PMID:26841762) (PMCID:PMC4741192)

Nakasone, M. and Huang, D. T. (2016) Ubiquitination accomplished: E1 and E2 enzymes were not necessary. Molecular Cell, 62(6), pp. 807-809. (doi: 10.1016/j.molcel.2016.06.001) (PMID:27315555)

2015

Buetow, L., Gabrielsen, M. , Anthony, N. G., Dou, H., Patel, A., Aitkenhead, H., Sibbet, G. J., Smith, B. O. and Huang, D. T. (2015) Activation of a primed RING E3-E2–ubiquitin complex by non-covalent ubiquitin. Molecular Cell, 58(2), pp. 297-310. (doi: 10.1016/j.molcel.2015.02.017) (PMID:25801170)

2013

Dou, H., Buetow, L., Sibbet, G.J., Cameron, K. and Huang, D.T. (2013) Essentiality of a non-RING element in priming donor ubiquitin for catalysis by a monomeric E3. Nature Structural and Molecular Biology, 20(8), pp. 982-986. (doi: 10.1038/nsmb.2621)

2012

Dou, H., Buetow, L., Hock, A., Sibbet, G.J., Vousden, K.H. and Huang, D.T. (2012) Structural basis for autoinhibition and phosphorylation-dependent activation of c-Cbl. Nature Structural and Molecular Biology, 19(2), pp. 184-192. (doi: 10.1038/nsmb.2231)

Dou, H., Buetow, L., Sibbet, G.J., Cameron, K. and Huang, D.T. (2012) BIRC7–E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nature Structural and Molecular Biology, 19(9), pp. 876-883. (doi: 10.1038/nsmb.2379)

2009

Huang, D. T. , Ayrault, O., Hunt, H. W., Taherbhoy, A. M., Duda, D. M., Scott, D. C., Borg, L. A., Neale, G., Murray, P. J. and Roussel, M. F. (2009) E2-RING Expansion of the NEDD8 Cascade Confers Specificity to Cullin Modification. Molecular Cell, 33(4), pp. 483-495. (doi: 10.1016/j.molcel.2009.01.011)

2008

Huang, D. T. , Zhuang, M., Ayrault, O. and Schulman, B. A. (2008) Identification of conjugation specificity determinants unmasks vestigial preference for ubiquitin within the NEDD8 E2. Nature Structural and Molecular Biology, 15(3), pp. 280-287. (doi: 10.1038/nsmb.1387)

2007

Huang, D. T. , Hunt, H. W., Zhuang, M., Ohi, M. D., Holton, J. M. and Schulman, B. A. (2007) Basis for a ubiquitin-like protein thioester switch toggling E1–E2 affinity. Nature, 445(7126), pp. 394-398. (doi: 10.1038/nature05490)

Articles

Vringer, E. et al. (2024) Mitochondrial outer membrane integrity regulates a ubiquitin-dependent and NF-κB-mediated inflammatory response. EMBO Journal, 43(6), pp. 904-930. (doi: 10.1038/s44318-024-00044-1) (PMID:38337057) (PMCID:PMC10943237)

Nikolatou, K. et al. (2023) PTEN deficiency exposes a requirement for an ARF GTPase module for integrin-dependent invasion in ovarian cancer. EMBO Journal, 42, e1139. (doi: 10.15252/embj.2023113987) (PMID:37577760) (PMCID:PMC10505920)

Villar, V. H. et al. (2023) Hepatic glutamine synthetase controls N5-methylglutamine in homeostasis and cancer. Nature Chemical Biology, 19(3), pp. 292-300. (doi: 10.1038/s41589-022-01154-9) (PMID:36280791) (PMCID:PMC9974483)

Schmidt, T. et al. (2023) eIF4A1-dependent mRNAs employ purine-rich 5’UTR sequences to activate localised eIF4A1-unwinding through eIF4A1-multimerisation to facilitate translation. Nucleic Acids Research, 51(4), pp. 1859-1879. (doi: 10.1093/nar/gkad030) (PMID:36727461) (PMCID:PMC9976904)

Chen, H. et al. (2023) PRL2 phosphatase enhances oncogenic FLT3 signaling via dephosphorylation of the E3 ubiquitin ligase CBL at tyrosine 371. Blood Vessels, 141(3), pp. 244-259. (doi: 10.1182/blood.2022016580) (PMID:36206490)

Kowalczyk, D., Nakasone, M. A., Smith, B. O. and Huang, D. T. (2022) Bivalent binding of p14ARF to MDM2 RING and acidic domains inhibits E3 ligase function. Life Science Alliance, 5(12), e202201472. (doi: 10.26508/lsa.202201472) (PMID:35944929) (PMCID:PMC9366199)

Nakasone, M. A., Majorek, K. A., Gabrielsen, M. , Sibbet, G. J., Smith, B. O. and Huang, D. T. (2022) Structure of UBE2K-Ub/E3/polyUb reveals mechanisms of K48-linked Ub chain extension. Nature Chemical Biology, 18, pp. 422-431. (doi: 10.1038/s41589-021-00952-x) (PMID:35027744) (PMCID:PMC8964413)

Ahmed, S. F., Buetow, L., Gabrielsen, M. , Lilla, S., Sibbet, G. J., Sumpton, D., Zanivan, S. , Hedley, A., Clark, W. and Huang, D. T. (2021) E3 ligase-inactivation rewires CBL interactome to elicit oncogenesis by hijacking RTK–CBL–CIN85 axis. Oncogene, 40(12), pp. 2149-2164. (doi: 10.1038/s41388-021-01684-x) (PMID:33627783) (PMCID:PMC7994203)

Magnussen, H. M. and Huang, D. T. (2021) Identification of a catalytic active but non-aggregating MDM2 RING domain variant. Journal of Molecular Biology, 433(5), 166807. (doi: 10.1016/j.jmb.2021.166807) (PMID:33450248) (PMCID:PMC7895813)

Humpton, T. J. et al. (2021) Differential requirements for MDM2 E3 activity during embryogenesis and in adult mice. Genes and Development, 35(1-2), pp. 117-132. (doi: 10.1101/gad.341875.120) (PMID:33334825) (PMCID:PMC7778261)

Chatrin, C., Gabrielsen, M. , Buetow, L., Nakasone, M. A., Ahmed, S. F., Sumpton, D., Sibbet, G. J., Smith, B. O. and Huang, D. T. (2020) Structural insights into ADP-ribosylation of ubiquitin by Deltex family E3 ubiquitin ligases. Science Advances, 6(38), eabc0418. (doi: 10.1126/sciadv.abc0418) (PMID:32948590) (PMCID:PMC7500938)

Ahmed, S. F., Buetow, L., Gabrielsen, M. , Lilla, S., Chatrin, C., Sibbet, G. J., Zanivan, S. and Huang, D. T. (2020) DELTEX2 C-terminal domain recognizes and recruits ADP-ribosylated proteins for ubiquitination. Science Advances, 6(34), eabc0629. (doi: 10.1126/sciadv.abc0629) (PMID:32937373) (PMCID:PMC7442474)

Magnussen, H. M. et al. (2020) Structural basis for DNA damage-induced phosphoregulation of MDM2 RING domain. Nature Communications, 11, 2094. (doi: 10.1038/s41467-020-15783-y) (PMID:32350255) (PMCID:PMC7190642)

Gabrielsen, M., Buetow, L., Kowalczyk, D., Zhang, W., Sidhu, S. S. and Huang, D. T. (2019) Identification and characterization of mutations in ubiquitin required for non-covalent dimer formation. Structure, 27(9), 1452-1459.e4. (doi: 10.1016/j.str.2019.06.008) (PMID:31303481) (PMCID:PMC6720194)

Patel, A., Sibbet, G. J. and Huang, D. T. (2019) Structural insights into non-covalent ubiquitin activation of the cIAP1-UbcH5B~ubiquitin complex. Journal of Biological Chemistry, 294, pp. 1240-1249. (doi: 10.1074/jbc.RA118.006045) (PMID:30523153) (PMCID:PMC6349121)

Marciano, G., Da Vela, S., Tria, G., Svergun, D. I., Byron, O. and Huang, D. T. (2018) Structure specific recognition protein-1 (SSRP1) is an elongated homodimer that binds histones. Journal of Biological Chemistry, 293(26), pp. 10071-10083. (doi: 10.1074/jbc.RA117.000994) (PMID:29764934) (PMCID:PMC6028955)

Gabrielsen, M. , Buetow, L., Nakasone, M. A., Ahmed, S. F., Sibbet, G. J., Smith, B. O. , Zhang, W., Sidhu, S. S. and Huang, D. T. (2017) A general strategy for discovery of inhibitors and activators of RING and U-box E3 ligases with ubiquitin variants. Molecular Cell, 68(2), 456-470.e10. (doi: 10.1016/j.molcel.2017.09.027) (PMID:29053960) (PMCID:PMC5655547)

Nomura, K. , Klejnot, M., Kowalczyk, D., Hock, A. K., Sibbet, G. J., Vousden, K. and Huang, D. T. (2017) Structural analysis of MDM2 RING separates degradation from regulation of p53 transcription activity. Nature Structural and Molecular Biology, 24(7), pp. 578-587. (doi: 10.1038/nsmb.3414) (PMID:28553961)

Buetow, L. and Huang, D. T. (2016) Structural insights into the catalysis and regulation of E3 ubiquitin ligases. Nature Reviews Molecular Cell Biology, 17(10), pp. 626-642. (doi: 10.1038/nrm.2016.91) (PMID:27485899)

Buetow, L., Tria, G., Ahmed, S. F., Hock, A., Dou, H., Sibbet, G. J., Svergun, D. I. and Huang, D. T. (2016) Casitas B-lineage lymphoma linker helix mutations found in myeloproliferative neoplasms affect conformation. BMC Biology, 14, 76. (doi: 10.1186/s12915-016-0298-6) (PMID:27609087) (PMCID:PMC5015263)

Marciano, G. and Huang, D.T. (2016) Structure of the human histone chaperone FACT Spt16 N-terminal domain. Acta Crystallographica. Section F: Structural Biology Communications, 72(2), pp. 121-128. (doi: 10.1107/s2053230x15024565) (PMID:26841762) (PMCID:PMC4741192)

Nakasone, M. and Huang, D. T. (2016) Ubiquitination accomplished: E1 and E2 enzymes were not necessary. Molecular Cell, 62(6), pp. 807-809. (doi: 10.1016/j.molcel.2016.06.001) (PMID:27315555)

Buetow, L., Gabrielsen, M. , Anthony, N. G., Dou, H., Patel, A., Aitkenhead, H., Sibbet, G. J., Smith, B. O. and Huang, D. T. (2015) Activation of a primed RING E3-E2–ubiquitin complex by non-covalent ubiquitin. Molecular Cell, 58(2), pp. 297-310. (doi: 10.1016/j.molcel.2015.02.017) (PMID:25801170)

Dou, H., Buetow, L., Sibbet, G.J., Cameron, K. and Huang, D.T. (2013) Essentiality of a non-RING element in priming donor ubiquitin for catalysis by a monomeric E3. Nature Structural and Molecular Biology, 20(8), pp. 982-986. (doi: 10.1038/nsmb.2621)

Dou, H., Buetow, L., Hock, A., Sibbet, G.J., Vousden, K.H. and Huang, D.T. (2012) Structural basis for autoinhibition and phosphorylation-dependent activation of c-Cbl. Nature Structural and Molecular Biology, 19(2), pp. 184-192. (doi: 10.1038/nsmb.2231)

Dou, H., Buetow, L., Sibbet, G.J., Cameron, K. and Huang, D.T. (2012) BIRC7–E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nature Structural and Molecular Biology, 19(9), pp. 876-883. (doi: 10.1038/nsmb.2379)

Huang, D. T. , Ayrault, O., Hunt, H. W., Taherbhoy, A. M., Duda, D. M., Scott, D. C., Borg, L. A., Neale, G., Murray, P. J. and Roussel, M. F. (2009) E2-RING Expansion of the NEDD8 Cascade Confers Specificity to Cullin Modification. Molecular Cell, 33(4), pp. 483-495. (doi: 10.1016/j.molcel.2009.01.011)

Huang, D. T. , Zhuang, M., Ayrault, O. and Schulman, B. A. (2008) Identification of conjugation specificity determinants unmasks vestigial preference for ubiquitin within the NEDD8 E2. Nature Structural and Molecular Biology, 15(3), pp. 280-287. (doi: 10.1038/nsmb.1387)

Huang, D. T. , Hunt, H. W., Zhuang, M., Ohi, M. D., Holton, J. M. and Schulman, B. A. (2007) Basis for a ubiquitin-like protein thioester switch toggling E1–E2 affinity. Nature, 445(7126), pp. 394-398. (doi: 10.1038/nature05490)

Book Sections

Buetow, L., Gabrielsen, M. and Huang, D. (2018) Single-Turnover RING/U-Box E3-Mediated Lysine Discharge Assays. In: Mayor, T. and Kleiger, G. (eds.) The Ubiquitin Proteasome System. Series: Methods in Molecular Biology (1844). Humana Press, pp. 19-31. ISBN 9781493987054 (doi: 10.1007/978-1-4939-8706-1_2)