Department of Plant Biology
Molecular mechanisms of signal transduction and their regulation by proteolytic pathways
Our lab integrates cutting edge approaches from the fields of structural biology, biochemistry, and molecular and cellular biology to decode sensing machineries and signaling pathways in plants, fungi, and humans. Our ultimate goal is to decipher fundamental biological pathways from the atomic to organismal level, and develop innovative strategies for the benefit of agriculture, environment, and human health. We are particularly interested in dissecting signaling pathways that are triggered by extracellular stimuli (such as light, gravity, small-molecules, hormones, and pathogens), and revealing their regulation by the ubiquitin-proteasome system.
Grad Group Affiliations
- Biochemistry, Molecular, Cellular and Developmental Biology
- Plant Biology
Specialties / Focus
- Cancer Biology
- Cell and Developmental Biology
- Cell Biology
- Cellular Responses to Toxins and Stress
- Developmental Biology
- Genomics, Proteomics and Metabolomics
- Molecular Biology, Biochemistry and Genomics
- Molecular Medicine
- Plant Molecular Biology
- Signal Transduction
- Structural Biology
- Postdoctoral fellow, University of Washington - Howard Hughes Medical Institute (2013-2018)
- PhD Biochemistry, Technion Israel-Institute of Technology (2006-2010)
Shabek, N., Ticchiarelli, F., Mao, H., Hinds, TR., Leyser, O. & Zheng, N. (2018). Structural plasticity of D3-D14 ubiquitin ligase in strigolactone signalling. Nature. DOI: 10.1038/s41586-018-0743-5
Shabek, N., Ruble, J., Hinds, TR., and Zheng, N. (2018). Structural insights into DDA1 function as a core component of the CRL4-DDB1 ubiquitin ligase. Cell Discovery. DOI: 10.1038/s41421-018-0064-8
Zheng, N., Shabek, N. (2017). Ubiquitin ligases: structure, function, and regulation. Annu Rev Biochem. 86, 129-157.
Shabek, N., Zheng, N. (2014). Plant ubiquitin ligases as signaling hubs. Nat Struct Mol Biol 21, 293-296.
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.
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.
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.
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.
Shabek, N., Ciechanover, A. (2010). The degradation of ubiquitin: the fate of the cellular reaper. Cell Cycle 9, 523-530.
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. Proc Natl Acad Sci U S A 106, 11907-11912.
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.