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Roles of XB130, a novel adaptor protein, in cancer

DOI: 10.1186/2043-9113-1-10

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Adaptor proteins are molecules of modular structures without enzymatic activity, composed of multiple protein-protein and/or protein-lipid interacting domains, through which they link signaling components to form macromolecular complexes and propagate cellular signals [1,2]. Depending on the functional role of the interacting partner and the specific biological event that is triggered by these interactions, adaptor proteins can participate in the regulation of different signaling pathways. A good example of how adaptor proteins are involved in signal transduction is the activation of c-Src protein-tyrosine kinases by adaptor proteins via protein-protein interactions. Adaptor proteins are also important to mediate signals initiated via receptor-tyrosine kinases in responses to extracellular stimuli [3,4], and together with non-receptor protein-tyrosine kinases to orchestrate the signal transduction elicited by either ligand receptor interactions or by cellular structure reorganization [5]. Further, a number of adaptor proteins have been demonstrated to regulate tumorigenesis. For example, actin filament associated protein (AFAP) is required for actin stress fiber formation and cell adhesion, and is critical for tumorigenic growth in prostate cancer [6,7]. Tyrosine kinase substrate 5 is a scaffolding adaptor protein with five Src homology (SH) 3 domains, co-localizes to podosomes and regulates migration and invasion of different human cancer cells [8,9]. These findings support a broader investigation of adaptor proteins on tumorigenesis and their potentiality as diagnostic biomarkers and therapeutic targets of cancer.During our studies aimed at the characterization of the AFAP [10-12], we cloned a novel 130 kDa protein, referred to as XB130 [13]. Our studies have indeed indicated that XB130 plays, as an adaptor, important roles in the regulation of signal transduction, cell proliferation, survival, motility and invasion [13-16]. In this review, we focus on studies rel


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