Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/125597
Title: GlcNAcylation of the Unique domain of Lyn A protein of the Src family
Other Titles: GlcNAcilació del domini únic de la proteïna Lyn A de la família Src
Author: Górriz López, Núria
Director: Pons Vallès, Miquel
Keywords: Proteïnes quinases
Fosforilació
NAD (Coenzim)
Treballs de fi de grau
Protein kinases
Phosphorylation
NAD (Coenzyme)
Bachelor's thesis
Issue Date: Jun-2018
Abstract: Lyn is a protein member of the Src family of non-receptor tyrosine kinases (SFK). These proteins are involved in cell signalling pathways related to cell growth, migration, invasion, and survival. Lyn mediates the induction of apoptosis. Lyn tyrosine kinase exists as two isoforms, Lyn A and Lyn B of 56 and 53 kDa, respectively. These isoforms differ by a 21-aa insert found in the N-terminal unique domain of Lyn A. In this research, the whole protein Lyn A will not be studied, the focus will be on the Unique and SH3 domain. O-GlcNAcylation is a post-translational modification that involves the attachment of single O-linked N-acetylglucosamine (O-GlcNAc) moieties to Ser and Thr residues of cytoplasmic, nuclear and mitochondrial proteins, by an enzymatic reaction with OGT enzyme. Phosphorylation can also target Ser and Thr residues, then, between O-GlcNAcylation and phosphorylation exists and intensive and complex interplay. O-GlcNAcylation has been proposed to function as a nutrient and stress sensor that regulates cellular processes. In this research, the O-GlcNAcylation of Lyn A will be studied by performing an enzymatic linked assay of NADH/NAD+. To do so, USH3LynA protein and OGT enzyme will be expressed by E. coli and purified
Note: Treballs Finals de Grau de Química, Facultat de Química, Universitat de Barcelona, Any: 2018, Tutor: Miquel Pons Vallès
URI: http://hdl.handle.net/2445/125597
Appears in Collections:Treballs Finals de Grau (TFG) - Química

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