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Structural basis of lenalidomide-induced CK1α degradation by the CRL4CRBN ubiquitin ligase
Thalidomide and its derivative lenalidomide bind the CRL4CRBN E3 ubiquitin ligase and target protein substrates for degradation; structural and functional data determined here show that casein kinase 1α and the lymphoid transcription factor Ikaros, the efficacy targets of lenalidomide in two different blood cancers, interact with the CRBN–lenalidomide interface through a β-hairpin destruction motif.
- Georg Petzold
- , Eric S. Fischer
- & Nicolas H. Thomä
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Article |
Lenalidomide induces ubiquitination and degradation of CK1α in del(5q) MDS
Lenalidomide, a derivative of thalidomide, is an effective drug for myelodysplastic syndrome; lenalidomide binds the CRL4CRBN E3 ubiquitin ligase and promotes degradation of casein kinase 1a, on which the malignant cells rely for survival.
- Jan Krönke
- , Emma C. Fink
- & Benjamin L. Ebert
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Article |
Frequent pathway mutations of splicing machinery in myelodysplasia
- Kenichi Yoshida
- , Masashi Sanada
- & Seishi Ogawa