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|Title:||c-Abl, an accomplice in mutant p53 gain-of-function?||Authors:||Liu, Di||Keywords:||DRNTU::Science||Issue Date:||2014||Abstract:||Accumulating evidence indicates that mutant p53 (mutp53) has further effects on cancer cells apart from causing the loss of wild type p53 (wtp53) tumour suppressor functions. The pro-metastatic functions of mutant p53 (mutp53) result in a worse prognosis and are often lethal. Although mutp53 is well-characterized for its gain-of- function (GOF), the underlying mechanisms of the GOF remains poorly understood. Therefore, it is important to investigate the molecular mechanisms mediating these pro-oncogenic functions. Towards this goal, the Abelson tyrosine kinase (c-Abl) was identified as a potential accomplice in mediating mutp53 GOF. Using siRNA knockdown we have identified a role of mutp53 in influencing the cellular localization and stability of the c-Abl protein. However, as coimmunoprecipitation and Duolink in situ proximity ligation assay (Duolink PLA) do not seem to suggest an association between them, it is possible that the mutp53 regulation of c-Abl protein stability occurs via an indirect mechanism. Further work to investigate the binding, localization and functional changes of these proteins will provide a clearer picture of c-Abl’s involvement in mutp53 GOF and may facilitate the discovery of therapeutic drugs for the benefit of cancer patients.||URI:||http://hdl.handle.net/10356/60624||Rights:||Nanyang Technological University||Fulltext Permission:||restricted||Fulltext Availability:||With Fulltext|
|Appears in Collections:||SBS Student Reports (FYP/IA/PA/PI)|
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