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dc.contributor.authorHill, Sandra M
dc.contributor.authorWrobel, Lidia
dc.contributor.authorRubinsztein, David
dc.date.accessioned2018-12-22T00:31:54Z
dc.date.available2018-12-22T00:31:54Z
dc.date.issued2019-03
dc.identifier.issn1350-9047
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/287421
dc.description.abstractAutophagy is a conserved intracellular degradation pathway essential for protein homeostasis, survival and development. Defects in autophagic pathways have been connected to a variety of human diseases, including cancer and neurodegeneration. In the process of macroautophagy, cytoplasmic cargo is enclosed in a double-membrane structure and fused to the lysosome to allow for digestion and recycling of material. Autophagosome formation is primed by the ULK complex, which enables the downstream production of PI(3)P, a key lipid signalling molecule, on the phagophore membrane. The PI(3)P is generated by the PI3 kinase (PI3K) complex, consisting of the core components VPS34, VPS15 and Beclin 1. Beclin 1 is a central player in autophagy and constitutes a molecular platform for the regulation of autophagosome formation and maturation. Post-translational modifications of Beclin 1 affect its stability, interactions and ability to regulate PI3K activity, providing the cell with a plethora of strategies to fine-tune the levels of autophagy. Being such an important regulator, Beclin 1 is a potential target for therapeutic intervention and interfering with the post-translational regulation of Beclin 1 could be one way of manipulating the levels of autophagy. In this review, we provide an overview of the known post-translational modifications of Beclin 1 that govern its role in autophagy and how these modifications are maintained by input from several upstream signalling pathways. ▓.
dc.format.mediumPrint-Electronic
dc.languageeng
dc.publisherSpringer Science and Business Media LLC
dc.subjectPhagosomes
dc.subjectAnimals
dc.subjectHumans
dc.subjectPhosphatidylinositol Phosphates
dc.subjectSignal Transduction
dc.subjectProtein Processing, Post-Translational
dc.subjectPhosphorylation
dc.subjectAutophagy
dc.subjectUbiquitination
dc.subjectPhosphatidylinositol 3-Kinases
dc.subjectClass III Phosphatidylinositol 3-Kinases
dc.subjectAutophagy-Related Proteins
dc.subjectBeclin-1
dc.titlePost-translational modifications of Beclin 1 provide multiple strategies for autophagy regulation.
dc.typeArticle
prism.endingPage629
prism.issueIdentifier4
prism.publicationDate2019
prism.publicationNameCell Death Differ
prism.startingPage617
prism.volume26
dc.identifier.doi10.17863/CAM.34725
dcterms.dateAccepted2018-11-28
rioxxterms.versionofrecord10.1038/s41418-018-0254-9
rioxxterms.versionAM
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.licenseref.startdate2019-03
dc.contributor.orcidRubinsztein, David [0000-0001-5002-5263]
dc.identifier.eissn1476-5403
rioxxterms.typeJournal Article/Review
cam.issuedOnline2018-12-13
rioxxterms.freetoread.startdate2019-06-13


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