作者: Cui-Hua Liu , Xiao-Bo Qiu , Alfred L Goldberg
DOI:
关键词: Ubiquitin ligase 、 Inhibitor of apoptosis 、 Ubiquitin 、 Receptor tyrosine kinase 、 Deubiquitinating enzyme 、 Cell biology 、 Medicine 、 Ubiquitin-activating enzyme 、 Proteasome 、 Protein subunit
摘要: The ubiquitin-proteasome pathway (UPP) is the major system responsible for degradation of intracellular proteins in eukaryotes. By controlling levels key proteins, it regulates almost all cellular activities, including cell cycle progression, DNA replication and repair, transcription, protein quality control, immune response, apoptosis. UPP composed ubiquitination that marks proteasome which degrades ubiquitinated proteins. 26S a 2400 kDa complex consisting more than 40 subunits. Following catalyzed by ubiquitin activating enzyme (El), ubiquitin-carrier (E2), one cell's many ubiquitin-protein ligases (E3s), substrates are targeted to into small peptides. E3s regulate indirectly determining both specificity timing substrate ubiquitination, whereas deubiquitinating enzymes can inhibit this process releasing from substrates. In review, we attempt highlight recent progress research on its role regulation apoptosis focusing several important components, ubiqutin ligase Nrdp 1, ErbB/EGFR family receptor tyrosine kinases, BRUCE/Apollon (an Inhibitor Apoptosis Protein), novel subunit hRpnl3 (a binding site enzyme, UCH37).