Sato Y, Yamagata A, Ito S, Fukai S (Synchrotron Radiation Research Organization, Univ. of Tokyo) Goto E, Tokunaga F (IMCR, Gunma Univ.) Shibata Y, Inoue J (Institute of Medical Science, Univ. of Tokyo) Kubota Y, Takekawa M (Institute of Medical Science, Univ. of Tokyo)
About
The tumor suppressor CYLD belongs to a ubiquitin (Ub)-specific protease (USP) family deubiquitinase and specifically cleaves Met1- and Lys63-linked polyubiquitin chains to suppress inflammatory signaling pathways. In this study, crystal structures of CYLD for Met1- and Lys63-linked Ub chains and two distinct precatalytic states for Met1-linked chains were solved. Moreover, structure and functional relationship of CYLD on NF-kB and JNK signaling are revelaed.
Paper information
Structures of CYLD USP with Met1- or Lys63-linked diubiquitin reveal mechanisms for dual specificity.
Sato Y, Goto E, Shibata Y, Kubota Y, Yamagata A, Goto-Ito S, Kubota K, Inoue J, Takekawa M, Tokunaga F, Fukai S.
Nat Struct Mol Biol 22(3):222-229, 2015
Online URL
http://www.ncbi.nlm.nih.gov/pubmed/25686088
