TY - JOUR
T1 - Control of mitophagy initiation and progression by the TBK1 adaptors NAP1 and SINTBAD
AU - Adriaenssens, Elias
AU - Nguyen, Thanh Ngoc
AU - Sawa-Makarska, Justyna
AU - Khuu, Grace
AU - Schuschnig, Martina
AU - Shoebridge, Stephen
AU - Skulsuppaisarn, Marvin
AU - Watts, Emily Maria
AU - Csalyi, Kitti Dora
AU - Padman, Benjamin Scott
AU - Lazarou, Michael
AU - Martens, Sascha
N1 - Publisher Copyright:
© The Author(s) 2024.
PY - 2024/11
Y1 - 2024/11
N2 - Mitophagy preserves overall mitochondrial fitness by selectively targeting damaged mitochondria for degradation. The regulatory mechanisms that prevent PTEN-induced putative kinase 1 (PINK1) and E3 ubiquitin ligase Parkin (PINK1/Parkin)-dependent mitophagy and other selective autophagy pathways from overreacting while ensuring swift progression once initiated are largely elusive. Here, we demonstrate how the TBK1 (TANK-binding kinase 1) adaptors NAP1 (NAK-associated protein 1) and SINTBAD (similar to NAP1 TBK1 adaptor) restrict the initiation of OPTN (optineurin)-driven mitophagy by competing with OPTN for TBK1. Conversely, they promote the progression of nuclear dot protein 52 (NDP52)-driven mitophagy by recruiting TBK1 to NDP52 and stabilizing its interaction with FIP200. Notably, OPTN emerges as the primary recruiter of TBK1 during mitophagy initiation, which in return boosts NDP52-mediated mitophagy. Our results thus define NAP1 and SINTBAD as cargo receptor rheostats, elevating the threshold for mitophagy initiation by OPTN while promoting the progression of the pathway once set in motion by supporting NDP52. These findings shed light on the cellular strategy to prevent pathway hyperactivity while still ensuring efficient progression.
AB - Mitophagy preserves overall mitochondrial fitness by selectively targeting damaged mitochondria for degradation. The regulatory mechanisms that prevent PTEN-induced putative kinase 1 (PINK1) and E3 ubiquitin ligase Parkin (PINK1/Parkin)-dependent mitophagy and other selective autophagy pathways from overreacting while ensuring swift progression once initiated are largely elusive. Here, we demonstrate how the TBK1 (TANK-binding kinase 1) adaptors NAP1 (NAK-associated protein 1) and SINTBAD (similar to NAP1 TBK1 adaptor) restrict the initiation of OPTN (optineurin)-driven mitophagy by competing with OPTN for TBK1. Conversely, they promote the progression of nuclear dot protein 52 (NDP52)-driven mitophagy by recruiting TBK1 to NDP52 and stabilizing its interaction with FIP200. Notably, OPTN emerges as the primary recruiter of TBK1 during mitophagy initiation, which in return boosts NDP52-mediated mitophagy. Our results thus define NAP1 and SINTBAD as cargo receptor rheostats, elevating the threshold for mitophagy initiation by OPTN while promoting the progression of the pathway once set in motion by supporting NDP52. These findings shed light on the cellular strategy to prevent pathway hyperactivity while still ensuring efficient progression.
UR - http://www.scopus.com/inward/record.url?scp=85196783651&partnerID=8YFLogxK
U2 - 10.1038/s41594-024-01338-y
DO - 10.1038/s41594-024-01338-y
M3 - Article
C2 - 38918639
AN - SCOPUS:85196783651
SN - 1545-9993
VL - 31
SP - 1717
EP - 1731
JO - Nature Structural and Molecular Biology
JF - Nature Structural and Molecular Biology
IS - 11
ER -