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Structural Basis of Selective Ubiquitination of TRF1 by SCFFbx4
Authors:Zhixiong Zeng  Wei Wang  Yuting Yang  Yong Chen  Xiaomei Yang  J Alan Diehl  Xuedong Liu  Ming Lei
Institution:1. Howard Hughes Medical Institute, University of Michigan Medical School, 1150 West Medical Center Drive, Ann Arbor, MI 48109, USA;2. Department of Biological Chemistry, University of Michigan Medical School, 1150 West Medical Center Drive, Ann Arbor, MI 48109, USA;3. Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA;4. School of Life Science, Shandong University, Shanda Nanlu 27, Jinan, 250100, People''s Republic of China;5. The Leonard and Madlyn Abramson Family Cancer Research Institute and Cancer Center, University of Pennsylvania, Philadelphia, PA 19104, USA;6. Department of Cancer Biology, University of Pennsylvania, Philadelphia, PA 19104, USA
Abstract:
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  • Highlights? SCF ubiquitin ligase subunit Fbx4 binds TRF1 using an atypical small GTPase fold ? Fbx4 recognizes a globular domain of TRF1, not just short phosphorylated degrons ? Telomere shelterin component TIN2 competes with Fbx4 for TRF1 binding ? TIN2 and SCFFbx4 thus control TRF1 ubiquitination and degradation
    Keywords:
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