Abstract：
:The DDB1-CUL4-RBX1 (CRL4) ubiquitin ligase family regulates a diverse set of cellular pathways through dedicated substrate receptors (DCAFs). The DCAF DDB2 detects UV-induced pyrimidine dimers in the genome and facilitates nucleotide excision repair. We provide the molecular basis for DDB2 receptor-mediated cyclobutane pyrimidine dimer recognition in chromatin. The structures of the fully assembled DDB1-DDB2-CUL4A/B-RBX1 (CRL4(DDB2)) ligases reveal that the mobility of the ligase arm creates a defined ubiquitination zone around the damage, which precludes direct ligase activation by DNA lesions. Instead, the COP9 signalosome (CSN) mediates the CRL4(DDB2) inhibition in a CSN5 independent, nonenzymatic, fashion. In turn, CSN inhibition is relieved upon DNA damage binding to the DDB2 module within CSN-CRL4(DDB2). The Cockayne syndrome A DCAF complex crystal structure shows that CRL4(DCAF(WD40)) ligases share common architectural features. Our data support a general mechanism of ligase activation, which is induced by CSN displacement from CRL4(DCAF) on substrate binding to the DCAF.
journal_name
Celljournal_title
Cellauthors
Fischer ES,Scrima A,Böhm K,Matsumoto S,Lingaraju GM,Faty M,Yasuda T,Cavadini S,Wakasugi M,Hanaoka F,Iwai S,Gut H,Sugasawa K,Thomä NHdoi
10.1016/j.cell.2011.10.035subject
Has Abstractpub_date
2011-11-23 00:00:00pages
1024-39issue
5eissn
0092-8674issn
1097-4172pii
S0092-8674(11)01285-2journal_volume
147pub_type
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