Selected Publications and Preprints
Sun, F*., Palayam, M*., and Shabek, N (2022). Structure of maize BZR1-type β-amylase BAM8 provides new insights into its noncatalytic adaptation. Journal of Structural Biology LINK and biorxiv
Tal, L., Palayam, M., Ron, M., Young, A., Britt, A., and Shabek, N (2022). A conformational switch in the SCF-D3/MAX2 ubiquitin ligase facilitates strigolactone signaling. Nature Plants. nature.com/articles/s41477-022-01145-7 Full text: LINK (mentioned in the press )
Hand, AK., Shabek, N (2022). The Role of E3 Ubiquitin Ligases in Chloroplast Function. Preprint
Trenner, J., Monaghan, J., Saeed, B., Quint, M*., Shabek, N*., and Trujillo, M* (2022). Evolution and Functions of Plant U-box proteins (PUBs): From protein quality control to signalling. Annual Reviews of Plant Biology. annurev-arplant-102720-012310
A KARRIKIN INSENSITIVE2 paralog in lettuce mediates highly sensitive germination responses to karrikinolide. Plant Physiology.Guercio, AM., Salar, T., Cornu, D., Bendahmane, A., Boyer, FD., Rameau, C., Gutjahr, C., de Saint Germain, A*., and Shabek, N* (2022). Structural and Functional Analyses Explain Pea KAI2 Receptor Diversity and Reveal Stereoselective Catalysis During Signal Perception. (mentioned in the press )
Yadav, B., Jogawat, A., Lal, SK., Lakra, N., Mehta, S., Shabek, N., and Narayan OP (2021). Plant mineral transport systems and the potential for crop improvement. Planta doi.org/10.1007/s00425-020-03551-7
Sun, F., Ding, L., Feng, W., Cao, Y., Lu, F., Yang, Q., Li, W., Lu, Y., Shabek, N., Fu, F., and Yu, H (2020). Maize transcription factor ZmBES1/BZR1-5 positively regulates kernel size. Journal of Experimental Botany doi.org/10.1093/jxb
Kuppu, S., Marimuthu, M., Ron, M., Li, G., Huddleson, A., Siddeek, MH., Terry, J., Buchner, R., Shabek, N., Comai, L., and Britt, AB (2020). A variety of changes, including CRISPR/Cas9 mediated deletions, in CENH3 lead to uniparental genome elimination and haploid induction on outcrossing. Plant Biotechnology Journal. 10.1111/pbi.13365
Tal, L., Anleu-Gil, MX., Guercio, AM., and Shabek, N (2020). Structural Aspects of Plant Hormone Signal Perception and Regulation by Ubiquitin Ligases. Plant Physiology. 10.1104/pp.19.01282
Shabek, N., Ticchiarelli, F., Mao, H., Hinds, TR., Leyser, O. & Zheng, N. (2018). Structural plasticity of D3-D14 Ub ligase in strigolactone signalling. Nature. 10.1038/s41586-018-0743-5
- SPOTLIGHT – Trends in Plant Science. Binding or Hydrolysis? How Does the Strigolactone Receptor Work? (2019). 10.1016/j.tplants.2019.05.001
- Mentioned in the press
Shabek, N., Ruble, J., Waston CJ, Garbutt KC, Hinds, TR., and Zheng, N. (2018). Structural insights into DDA1 function as a core component of the CRL4-DDB1 ubiquitin ligase. Nature – Cell Discovery. 10.1038/s41421-018-0064-8
Zheng, N., Shabek, N. (2017). Ubiquitin ligases: structure, function, and regulation. Annual Reviews Biochemistry. 86, 129-157. 10.1146/annurev-biochem-060815-014922
Shabek, N., Zheng, N. (2014). Plant ubiquitin ligases as signaling hubs. Nature Structure Molecular Biology 21, 293-296. 10.1038/nsmb.2804
Zhou, F., Lin, Q., Zhu, L., Ren, Y., Zhou, K., Shabek, N., et al. (2013). D14-SCF(D3)-dependent degradation of D53 regulates strigolactone signaling. Nature. 504, 406-410. 10.1038/nature12878
Shabek, N., Herman-Bachinsky, Y., Buchsbaum, S., Lewinson, O., Haj-Yahya, M., Hejjaoui, M., Lashuel, HA., Sommer, T., Brik, A., and Ciechanover, A. (2012). The Size of the Proteasomal Substrate Determines Whether Its Degradation Will Be Mediated by Mono- or Polyubiquitylation. Mol Cell. 48, 87-97. 10.1016/j.molcel.2012.07.011.
- RESEARCH HIGHLIGHT – Nature Reviews Molecular Cell Biology. Protein Metabolism: Length Matters (2012). doi.org/10.1038/nrm3445
Braten O., Shabek, N., Kravtsova-Ivantsiv, Y., and Ciechanover, A. (2011). Generation of free ubiquitin chains is upregulated in stress, and facilitated by the HECT domain ubiquitin ligases, Ufd4 and Hul5. Biochem J. 444, 611-617. 10.1042/BJ20111840
Weissman, AM., Shabek, N., and Ciechanover, A. (2011). The predator becomes the prey: regulation of the ubiquitin system by ubiquitylation and degradation. Nat Rev Mol Cell Biol 12, 605-620. 10.1038/nrm3173
Shabek, N., Ciechanover, A. (2010). The degradation of ubiquitin: the fate of the cellular reaper. Cell Cycle 9, 523-530. 10.4161/cc.9.3.11152
Shabek, N., Herman-Bachinsky, Y., and Ciechanover, A. (2009). Ubiquitin degradation with its substrate, or as a monomer in a ubiquitination-independent mode, provides clues to proteasome regulation. PNAS 106, 11907-11912. 10.1073/pnas.0905746106
Shabek, N., Iwai, K., and Ciechanover, A. (2007). Ubiquitin is degraded by the ubiquitin system as a monomer and as part of its conjugated target. Biochem Biophys Res Commun 363, 425-431. 10.1016/j.bbrc.2007.08.185
Ivantsiv, Y., Kaplun, L., Tzirkin-Goldin, R., Shabek, N., and Raveh, D. (2006). Unique role for the UbL-UbA protein Ddi1 in turnover of SCFUfo1 complexes. Mol Cell Biol 26, 1579-1588. 10.1128/MCB.25.13.5355-5362.2005
Kaplun, L., Tzirkin, R., Bakhrat, A., Shabek, N., Ivantsiv, Y., and Raveh, D. (2005). The DNA damage-inducible UbL-UbA protein Ddi1 participates in Mec1-mediated degradation of Ho endonuclease. Mol Cell Biol 25, 5355-5362. 10.1128/MCB.25.13.5355-5362.2005
(* equal contribution)
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