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• W2062858030 abstract "Bcr-Abl, the causative agent of chronic myelogenous leukemia (CML), localizes in the cytoplasm where its oncogenic signaling leads to proliferation of cells. If forced into the nucleus Bcr-Abl causes apoptosis. To achieve nuclear translocation, binding domains for capture of Bcr-Abl were generated and attached to proteins with signals destined for the nucleus. These resulting proteins would be capable of binding and translocating endogenous Bcr-Abl to the nucleus.Bcr-Abl was targeted at 3 distinct domains for capture: by construction of high affinity intracellular antibody domains (iDabs) to regions of Bcr-Abl known to promote cytoplasmic retention, via its coiled coil domain (CC), and through a naturally occurring protein-protein interaction domain (RIN1). These binding domains were then tested for their ability to escort Bcr-Abl into the nucleus using a protein switch or attachment of 4 nuclear localization signals (NLSs).Although RIN1, ABI7-iDab, and CCmut3 constructs all produced similar colocalization with Bcr-Abl, only 4NLS-CCmut3 produced efficient nuclear translocation of Bcr-Abl.We demonstrate that a small binding domain can be used to control the subcellular localization of Bcr-Abl, which may have implications for CML therapy. Our ultimate future goal is to change the location of critical proteins to alter their function." @default.
• W2062858030 created "2016-06-24" @default.
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• W2062858030 date "2011-12-20" @default.
• W2062858030 modified "2023-10-18" @default.
• W2062858030 title "Changing the Subcellular Location of the Oncoprotein Bcr-Abl Using Rationally Designed Capture Motifs" @default.
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• W2062858030 doi "https://doi.org/10.1007/s11095-011-0654-8" @default.
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