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dc.contributor.advisorSeternes, Ole Morten
dc.contributor.advisorCzarna, Anna
dc.contributor.authorLuong, Bao Quoc
dc.date.accessioned2016-07-27T08:27:40Z
dc.date.available2016-07-27T08:27:40Z
dc.date.issued2016-05-12
dc.description.abstractThe mitogen-activated protein kinase 5 (MK5) binds to extracellular signal-regulated kinase 3 and 4(ERK3 and ERK4) through a unique FRIEDE motif in ERK3/4. 100 amino acids C-terminal in MK5 is sufficient for this binding. MK5s subcellular localization and activity is regulated by the atypical MAP kinase ERK3 and ERK4. In this project we wanted to express and purify full-length and different domains of MK5 and use it to gain structural information of the kinase to further reveal how it binds to ERK3 and ERK4 at the atomic level. Recombinant technics for generation of these proteins together with functional assays to assess the activity of MK5 have been used. Optimal protocols for expression and purification of the kinase was developed. Finally we used a GST pulldown assay to show that the amino acid domain amino acid domain 372-473 of MK5 are able to bind to ERK4 in extracts from mammalian cells.en_US
dc.identifier.urihttps://hdl.handle.net/10037/9487
dc.identifier.urnURN:NBN:no-uit_munin_9045
dc.language.isoengen_US
dc.publisherUiT Norges arktiske universiteten_US
dc.publisherUiT The Arctic University of Norwayen_US
dc.rights.accessRightsopenAccess
dc.rights.holderCopyright 2016 The Author(s)
dc.subject.courseIDFAR-3911
dc.subjectVDP::Matematikk og Naturvitenskap: 400::Basale biofag: 470::Molekylærbiologi: 473en_US
dc.subjectVDP::Mathematics and natural science: 400::Basic biosciences: 470::Molecular biology: 473en_US
dc.subjectVDP::Matematikk og Naturvitenskap: 400::Basale biofag: 470::Biokjemi: 476en_US
dc.subjectVDP::Mathematics and natural science: 400::Basic biosciences: 470::Biochemistry: 476en_US
dc.titleRegulation of ERK3/4 Function via Specific Protein-Protein Interactionsen_US
dc.typeMaster thesisen_US
dc.typeMastergradsoppgaveen_US


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