title: SUMOylation in carcinogenesis.
abstract: SUMOylation is a post-translational modification characterized by covalent and reversible binding of small ubiquitin-like modifier (SUMO) to a target protein. In mammals, four different isoforms, termed SUMO-1, -2, -3 and -4 have been identified so far. SUMO proteins are critically involved in the modulation of nuclear organization and cell viability. Their expression is significantly increased in processes associated with carcinogenesis such as cell growth, differentiation, senescence, oxidative stress and apoptosis. Little is known about the role of SUMOylation in cancer development. Therefore the present review focuses on possible implications of SUMOylation in carcinogenesis highlighting its impact as an important regulatory cell cycle protein. Moreover, novel opportunities for therapeutic approaches are discussed. The differential expression levels, the target protein preferences and the function of the SUMO pathway in different cancer subtypes raises unexpected issues questioning our understanding of the implication of SUMO in carcinogenesis.
authors.affiliation: Institute of Pathology, Medical University of Graz, Austria.
authors.forename: Kira
authors.initials: K
authors.lastname: Bettermann
authors.forename: Martin
authors.initials: M
authors.lastname: Benesch
authors.forename: Serge
authors.initials: S
authors.lastname: Weis
authors.forename: Johannes
authors.initials: J
authors.lastname: Haybaeck
mesh_terms: D000818:Animals; D002454:Cell Differentiation; D002471:Cell Transformation, Neoplastic / Q000378:metabolism*; D006801:Humans; D015398:Signal Transduction; D025841:Small Ubiquitin-Related Modifier Proteins / Q000378:metabolism*; D058207:Sumoylation / Q000502:physiology*; D025801:Ubiquitin / Q000235:genetics / Q000378:metabolism
chemical_list: D025841:Small Ubiquitin-Related Modifier Proteins; D025801:Ubiquitin