Olle Sangfelt's Group
Under normal circumstances, the activity of proteins is tightly regulated to ensure proper cell function. Proteins undergo extensive post-translational modifications (PTMs) that influence their stability and/or interaction with other proteins, as well as with RNAs and DNA molecules. One specific type of PTM is the covalent attachment of the small protein ubiquitin (Ub), in a process known as ubiquitylation.
Our research is focused on how protein ubiquitylation control cellular integrity and how alterations of components of the ubiquitin-machinery contribute to cancer development and progression. We use interdisciplinary high-throughput functional analysis in combination with biochemical studies to functionally characterize oncogenic SCF ligases and targets substrates. One of the main objectives of the research is to explore how specific signals converge to modulate SCF activity and substrate specificity and translate these discoveries into more effective treatments, for instance through identification of resistance-associated regulatory pathways that contribute to drug resistance and escape from targeted therapy. The basic research findings are also integrated with studies of human cancers for discovery of powerful prognostic/treatment predictive markers and novel combination therapies directed at SCF-driven molecular processes.
|Andrä Brunner||PhD student|
|Mohiuddin Gazi||Associated, Postdoc|
|Olle Sangfelt||Senior researcher|
|Aldwin Suryo Rahmanto||Postdoc|
FBW7 suppression leads to SOX9 stabilization and increased malignancy in medulloblastoma.
EMBO J. 2016 10;35(20):2192-2212
Proteomic screen reveals Fbw7 as a modulator of the NF-κB pathway.
Nat Commun 2012 ;3():976
Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line.
Nature 2001 Sep;413(6853):316-22