The novel mitochondrial outer membrane protein Mcp3 follows a unique IMP-dependent import pathway

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dc.contributor.advisor Rapaport, Doron (Prof. Dr.)
dc.contributor.author Sinzel, Monika Sonja
dc.date.accessioned 2017-12-21T09:22:40Z
dc.date.available 2017-12-21T09:22:40Z
dc.date.issued 2017-12-21
dc.identifier.other 49662220X de_DE
dc.identifier.uri http://hdl.handle.net/10900/79496
dc.identifier.uri http://nbn-resolving.de/urn:nbn:de:bsz:21-dspace-794963 de_DE
dc.identifier.uri http://dx.doi.org/10.15496/publikation-20894
dc.description.abstract Mitochondria are essential organelles of most eukaryotic cells and are involved in many important cellular activities. The viability of cells greatly depends on proper function of mitochondria, not only because mitochondria are ‘the powerhouse of the cell’, in fact they also play essential roles in metabolic processes and cellular signaling. Many neurological diseases are associated with mitochondrial disorders, illustrating the need to identify new components that participate in maintaining mitochondrial integrity. Mitochondria harbor two membranes, the mitochondrial outer membrane and inner membrane, which both have a characteristic phospholipid composition distinguishing them from all other cellular membranes. Maintenance of cellular and mitochondrial lipid homeostasis depends on membrane contact sites and the exchange of phospholipids between organelles. In yeast, connections between mitochondria and the endoplasmic reticulum (ER) are mediated by the ER-mitochondria encounter structure (ERMES) which has a crucial role in many cellular processes. Defects in ERMES lead to a multitude of phenotypes, but the precise molecular function of the ERMES complex and its subunit Mdm10 (mitochondrial distribution and morphology 10) is still not entirely understood. In order to shed light on this topic we searched for suppressors of the mdm10Δ growth defect and found a novel mitochondrial protein which we named Mcp3 for Mdm10 complementing protein 3. Mcp3 follows a unique biogenesis pathway. It is initially recognized by the mitochondrial import receptor Tom70 and crosses the outer membrane via the translocase of the outer membrane. Mcp3 is then handed over to the translocase of the inner membrane (TIM23) and gets processed by the inner membrane peptidase. Subsequently, mature Mcp3 is released to the intermembrane space and integrates into the outer membrane in a process that possibly involves the mitochondrial import complex. Mcp3 is the first outer membrane protein that is reported to be processed by a peptidase of the inner membrane and therefore follows a novel biogenesis pathway. en
dc.language.iso en de_DE
dc.publisher Universität Tübingen de_DE
dc.rights ubt-podok de_DE
dc.rights.uri http://tobias-lib.uni-tuebingen.de/doku/lic_mit_pod.php?la=de de_DE
dc.rights.uri http://tobias-lib.uni-tuebingen.de/doku/lic_mit_pod.php?la=en en
dc.subject.classification Mitochondrium de_DE
dc.subject.ddc 500 de_DE
dc.title The novel mitochondrial outer membrane protein Mcp3 follows a unique IMP-dependent import pathway en
dc.type PhDThesis de_DE
dcterms.dateAccepted 2017-12-04
utue.publikation.fachbereich Biochemie de_DE
utue.publikation.fakultaet 7 Mathematisch-Naturwissenschaftliche Fakultät de_DE

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