Selected Publications and Preprints

Tal, L., Guercio, AM., Varshney, K., Young, A., Gutjahr, C., and Shabek, N. (2023). C-terminal conformational changes in SCF-D3/MAX2 ubiquitin ligase are required for KAI2-mediated signaling (biorxiv LINK)

Guercio, AM*., Palayam, M*., and Shabek, N (2023). Strigolactones: Diversity, Perception, and Hydrolysis. Phytochemistry Reviews. LINK

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 (selected for JSB Cover Page, Volume 214, 3)

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 media )

Hand, AK., Shabek, N (2022). The Role of E3 Ubiquitin Ligases in Chloroplast Function. International Journal of Molecular Sciences. LINK

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

Martinez, SE., Conn, CE., Guercio, AM., Sepulveda, C., Fiscus, CJ., Koenig, D., Shabek, N., Nelson, DC (2022). A KARRIKIN INSENSITIVE2 paralog in lettuce mediates highly sensitive germination responses to karrikinolide. Plant Physiology. LINK

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. Communications Biology – Nature. https://www.nature.com/articles/s42003-022-03085-6   (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

Palayam, M., Ganapathy, J., Guercio, AM., Tal, L., Deck, SL., and Shabek, N (2021). Structural Insights into Photoactivation of Plant Cryptochrome-2.  Communications Biology – Nature  doi. 10.1038/s42003-020-01531-x /     (mentioned in the press )

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

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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