Shuttling of PINK1 between Mitochondrial Microcompartments Resolved by Triple-Color Superresolution Microscopy

DC FieldValueLanguage
dc.contributor.authorBeinlich, Felix R. M.
dc.contributor.authorDrees, Christoph
dc.contributor.authorPiehler, Jacob
dc.contributor.authorBusch, Karin B.
dc.date.accessioned2021-12-23T16:04:42Z-
dc.date.available2021-12-23T16:04:42Z-
dc.date.issued2015
dc.identifier.issn15548929
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/6560-
dc.description.abstractThe cytosolic phosphatase and tensin homologue Pten-kinase PINK1 involved in mitochondrial quality control undergoes a proteolytic process inside mitochondria. It has been suggested that the protein is not fully imported into mitochondria during this maturation. Here, we have established live cell triple-color superresolution microscopy by combining FPALM and tracking and localization microscopy (TALM) in order to unravel the spatiotemporal organization of the C-terminal kinase domain of PINKI during this process. We find that the kinase domain is imported into active mitochondria and colocalizes with respiratory complex I at the inner mitochondrial membrane. When the processing step inside mitochondria is inhibited or mitochondria are de-energized, full length PINK1 distributes between the outer and the inner mitochondrial membranes, indicating a holdup of import. These findings give the molecular base for a dual role of PINK1-inside energized mitochondria and outside of de-energized mitochondria.
dc.description.sponsorshipGerman National Research FoundationGerman Research Foundation (DFG) [Bu2288/1-2, SFB944]; The SIR-<SUP>BG</SUP> was a kind gift of K. Johnsson. We thank Christian Richter for the development of image analysis software, Rainer Kurre for technical support with the microscopic set-up and Wladislaw Kohl for technical assistance. This work was supported by the German National Research Foundation grant Bu2288/1-2 and the SFB944.
dc.language.isoen
dc.publisherAMER CHEMICAL SOC
dc.relation.ispartofACS CHEMICAL BIOLOGY
dc.subjectBiochemistry & Molecular Biology
dc.subjectCLEAVAGE
dc.subjectCOMPLEX
dc.subjectIMPORT
dc.subjectKINASE
dc.subjectMEMBRANE
dc.subjectMITOPHAGY
dc.subjectORGANIZATION
dc.subjectPATHWAY
dc.subjectPROTEINS
dc.subjectTRACKING
dc.titleShuttling of PINK1 between Mitochondrial Microcompartments Resolved by Triple-Color Superresolution Microscopy
dc.typejournal article
dc.identifier.doi10.1021/acschembio.5b00295
dc.identifier.isiISI:000361867200004
dc.description.volume10
dc.description.issue9
dc.description.startpage1970
dc.description.endpage1976
dc.contributor.orcid0000-0003-0525-0191
dc.contributor.researcheridABH-8594-2020
dc.contributor.researcheridAAM-8374-2021
dc.identifier.eissn15548937
dc.publisher.place1155 16TH ST, NW, WASHINGTON, DC 20036 USA
dcterms.isPartOf.abbreviationACS Chem. Biol.
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.orcid0000-0002-2143-2270-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidPiJa938-
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