The role of the individual TOM subunits in the association of PINK1 with depolarized mitochondria

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URI: http://hdl.handle.net/10900/127720
http://nbn-resolving.de/urn:nbn:de:bsz:21-dspace-1277208
http://dx.doi.org/10.15496/publikation-69083
http://nbn-resolving.org/urn:nbn:de:bsz:21-dspace-1277200
http://nbn-resolving.org/urn:nbn:de:bsz:21-dspace-1277207
Dokumentart: PhDThesis
Date: 2022-06-02
Language: English
Faculty: 7 Mathematisch-Naturwissenschaftliche Fakultät
Department: Biochemie
Advisor: Rapaport, Doron (Prof. Dr.)
Day of Oral Examination: 2022-05-24
DDC Classifikation: 570 - Life sciences; biology
License: http://tobias-lib.uni-tuebingen.de/doku/lic_mit_pod.php?la=de http://tobias-lib.uni-tuebingen.de/doku/lic_mit_pod.php?la=en
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Inhaltszusammenfassung:

Mitochondria dysfunction is involved in the pathomechanism of many illnesses including Parkinson’s disease. PINK1, which is mutated in some cases of familial Parkinsonism, is a key component in the degradation of damaged mitochondria by mitophagy. The accumulation of PINK1 on the mitochondrial outer membrane (MOM) of compromised organelles is crucial for the induction of mitophagy, but the molecular mechanism of this process is still unresolved. Here, we investigate the association of PINK1 with the TOM complex. We demonstrate that PINK1 heavily relies on the import receptor TOM70 for its association with mitochondria and directly interacts with this receptor. The structural protein TOM7 appears to play only a moderate role in PINK1 association with the TOM complex, probably due to its role in stabilizing this complex. PINK1 requires the TOM40 pore lumen for its stable interaction with the TOM complex and apparently remains there during its further association with the MOM. Overall, this study provides new insights on the role of the individual TOM subunits in the association of PINK1 with the MOM of depolarized mitochondria.

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