Ontology highlight
ABSTRACT:
SUBMITTER: Choi WH
PROVIDER: S-EPMC4786872 | biostudies-literature | 2016 Mar
REPOSITORIES: biostudies-literature
Choi Won Hoon WH de Poot Stefanie A H SA Lee Jung Hoon JH Kim Ji Hyeon JH Han Dong Hoon DH Kim Yun Kyung YK Finley Daniel D Lee Min Jae MJ
Nature communications 20160309
When in the closed form, the substrate translocation channel of the proteasome core particle (CP) is blocked by the convergent N termini of α-subunits. To probe the role of channel gating in mammalian proteasomes, we deleted the N-terminal tail of α3; the resulting α3ΔN proteasomes are intact but hyperactive in the hydrolysis of fluorogenic peptide substrates and the degradation of polyubiquitinated proteins. Cells expressing the hyperactive proteasomes show markedly elevated degradation of many ...[more]