FIP200 Phosphorylation Regulates Late Steps in Mitophagy
Abstract
Mitophagy is a specific type of autophagy responsible for the selective elimination of dysfunctional or superfluous mitochondria, ensuring the maintenance of mitochondrial quality control. The initiation of mitophagy is coordinated by the ULK1 kinase complex, which engages mitophagy receptors via its FIP200 subunit. Whether FIP200 performs additional functions in the subsequent later phases of mitophagy beyond this initial step and how its regulation occurs, remains unclear. Our findings reveal that multiple phosphorylation events on FIP200 differentially control the early and late stages of mitophagy. Furthermore, these phosphorylation events influence FIP200's interaction with ATG16L1. In summary, our results highlight the necessity for precise and dynamic regulation of FIP200, underscoring its importance in the progression of mitophagy.
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BibTeX
@article{eickhorst2026fip200,
title = {{FIP200 Phosphorylation Regulates Late Steps in Mitophagy}},
author = {Christopher Eickhorst and Riccardo Babic and Jorrell Rush-Kittle and Leon Lucya and Fatimah Lami Imam and Pablo Sánchez-Martín and David Hollenstein and Jonas Michaelis and Christian Münch and Chris Meisinger and Dea Slade and Laura Gámez-Díaz and Claudine Kraft},
journal = {Journal of Molecular Biology},
year = {2026},
month = oct,
doi = {10.1016/j.jmb.2024.168631},
url = {https://hal.science/hal-05787674v1},
note = {CC BY},
}
RIS
TY - JOUR
TI - FIP200 Phosphorylation Regulates Late Steps in Mitophagy
AU - Christopher Eickhorst
AU - Riccardo Babic
AU - Jorrell Rush-Kittle
AU - Leon Lucya
AU - Fatimah Lami Imam
AU - Pablo Sánchez-Martín
AU - David Hollenstein
AU - Jonas Michaelis
AU - Christian Münch
AU - Chris Meisinger
AU - Dea Slade
AU - Laura Gámez-Díaz
AU - Claudine Kraft
PY - 2026
DA - 2026/10/08
JO - Journal of Molecular Biology
DO - 10.1016/j.jmb.2024.168631
UR - https://hal.science/hal-05787674v1
AB - Mitophagy is a specific type of autophagy responsible for the selective elimination of dysfunctional or superfluous mitochondria, ensuring the maintenance of mitochondrial quality control. The initiation of mitophagy is coordinated by the ULK1 kinase complex, which engages mitophagy receptors via its FIP200 subunit. Whether FIP200 performs additional functions in the subsequent later phases of mitophagy beyond this initial step and how its regulation occurs, remains unclear. Our findings reveal that multiple phosphorylation events on FIP200 differentially control the early and late stages of mitophagy. Furthermore, these phosphorylation events influence FIP200's interaction with ATG16L1. In summary, our results highlight the necessity for precise and dynamic regulation of FIP200, underscoring its importance in the progression of mitophagy.
SN - 0022-2836
SN - 1089-8638
ER -