Yun-Erh Kuan
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Yun-Erh Kuan has a total of 3 co-authors. Here are the top co-authors by number of shared publications:
- Chung-I Chang
Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan
1 shared publication - Hsiu-Jung Wang
Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan
1 shared publication - Meng-Ru Ho
Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan
1 shared publication
Latest Publications
- Open Access
- 5 March 2025
- Published by Springer Nature in Nature Communications
- Vol. 16 (1) , 1-9
Structural basis for the allosteric activation of Lon by the heat shock protein LarA
Lon is a conserved AAA+ (ATPases associated with diverse cellular activities) proteolytic machine that plays a key regulatory role in cells under proteotoxic stress. Lon-mediated proteolysis can be stimulated by either the unfolded or specific protein substrates accumulated under stress conditions. However, the molecular basis for this substrate-controlled proteolysis remains unclear. Here, we have found that the heat shock protein LarA, a recently discovered Lon substrate and allosteric activator, binds to the N-terminal domain (NTD) of Lon. The crystal structure of the LarA-NTD complex shows that LarA binds to a highly conserved groove in the NTD through the terminal aromatic residue of its C-terminal degron. Crystallographic and biochemical evidence further reveals that this binding exposes the hydrophobic core of LarA, which can bind a leucine residue and promote local protein unfolding. These results define the mechanistic role of the NTD in regulating Lon-mediated proteolysis in response to varying cellular conditions.
- 5 March 2025
- Published by Springer Nature in Nature Communications
- Vol. 16 (1) , 1-9
Open AccessStructural basis for the allosteric activation of Lon by the heat shock protein LarA
Lon is a conserved AAA+ (ATPases associated with diverse cellular activities) proteolytic machine that plays a key regulatory role in cells under proteotoxic stress. Lon-mediated proteolysis can be stimulated by either the unfolded or specific protein substrates accumulated under stress conditions. However, the molecular basis for this substrate-controlled proteolysis remains unclear. Here, we have found that the heat shock protein LarA, a recently discovered Lon substrate and allosteric activator, binds to the N-terminal domain (NTD) of Lon. The crystal structure of the LarA-NTD complex shows that LarA binds to a highly conserved groove in the NTD through the terminal aromatic residue of its C-terminal degron. Crystallographic and biochemical evidence further reveals that this binding exposes the hydrophobic core of LarA, which can bind a leucine residue and promote local protein unfolding. These results define the mechanistic role of the NTD in regulating Lon-mediated proteolysis in response to varying cellular conditions.