{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Fujita K"],"funding":["Nagoya Daigaku","Japan Science and Technology Agency","Ministry of Education, Culture, Sports, Science and Technology of Japan"],"pagination":["jcs260395"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9789397"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["135(23)"],"pubmed_abstract":["Mitophagy, a type of selective autophagy, specifically targets damaged mitochondria. The ULK complex regulates Parkin-mediated mitophagy, but the mechanism through which the ULK complex initiates mitophagosome formation remains unknown. The Rab7 GTPase (herein referring to Rab7a) is a key initiator of mitophagosome formation, and Ser-72 phosphorylation of Rab7 is important for this process. We have previously identified LRRK1 as a protein kinase responsible for Rab7 Ser-72 phosphorylation. In this study, we investigated the role of LRRK1 in mitophagy. We showed that LRRK1 functions downstream of ULK1 and ULK2 in Parkin-mediated mitophagy. Furthermore, we demonstrated that ectopic targeting of active LRRK1 to mitochondria is sufficient to induce the Ser-72 phosphorylation of Rab7, circumven"],"journal":["Journal of cell science"],"pubmed_title":["The ULK complex-LRRK1 axis regulates Parkin-mediated mitophagy via Rab7 Ser-72 phosphorylation."],"pmcid":["PMC9789397"],"funding_grant_id":["JPMJMS2024"],"pubmed_authors":["Kedashiro S","Hisamoto N","Yagi T","Matsumoto K","Hanafusa H","Fujita K"],"additional_accession":[]},"is_claimable":false,"name":"The ULK complex-LRRK1 axis regulates Parkin-mediated mitophagy via Rab7 Ser-72 phosphorylation.","description":"Mitophagy, a type of selective autophagy, specifically targets damaged mitochondria. The ULK complex regulates Parkin-mediated mitophagy, but the mechanism through which the ULK complex initiates mitophagosome formation remains unknown. The Rab7 GTPase (herein referring to Rab7a) is a key initiator of mitophagosome formation, and Ser-72 phosphorylation of Rab7 is important for this process. We have previously identified LRRK1 as a protein kinase responsible for Rab7 Ser-72 phosphorylation. In this study, we investigated the role of LRRK1 in mitophagy. We showed that LRRK1 functions downstream of ULK1 and ULK2 in Parkin-mediated mitophagy. Furthermore, we demonstrated that ectopic targeting of active LRRK1 to mitochondria is sufficient to induce the Ser-72 phosphorylation of Rab7, circumven","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2025-04-26T09:57:32.079Z","creation":"2025-04-06T13:09:55.969Z"},"accession":"S-EPMC9789397","cross_references":{"pubmed":["36408770"],"doi":["10.1242/jcs.260395"]}}