Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 468, Issue 1-2, Pages 143-150Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2015.10.144
Keywords
Proteasome; Inhibitor; Peptide; Coiled-coil; Protein degradation; Rpt subunit
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Funding
- Ministry of Education, Culture, Sports, Science and Technology
- Grants-in-Aid for Scientific Research [15H01531, 26870216] Funding Source: KAKEN
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Regulation of proteasomal degradation is an indispensable tool for biomedical studies. Thus, there is demand for novel proteasome inhibitors. Proteasomal degradation requires formation of coiled-coil structure by the N-terminal region of ATPase subunits of the proteasome cap. Here we show that peptides that mimic the N-terminal coiled-coil region of ATPase subunits interfere with proteasome function. These results suggest that coiled-coil peptides represent promising new proteasome inhibitors and that N-terminal coiled-coil regions of ATPase subunits are targets for proteasome inhibition. (C) 2015 Elsevier Inc. All rights reserved.
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