Method for targeting degradation of intracellular proteins
AssigneeThe Regents of the University of California
InventorsPhilip Coffino, Xianqiang Li
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Abstract
A method for selective targeted degradation of intracellular proteins in situ by inducing in cells a production of an agent comprising N-terminal domain as well as a C-terminal domain. The N-terminal domain destabilizes the target protein and directs its degradation when attached to it through the C-terminal domain acting as a linker between the target protein and between the protein agent of the invention. The protein degradation directing N-terminal domain is a subregion within 97 amino acids corresponding to the N-terminus of protein antizyme.
Claims6
A method for in vitro intracellular ubiquitin independent degradation of a target protein which can be covalently or non-covalently linked to N-terminal domain of antizyme in cells of a mammal subject in need of such target protein degradation, said method comprising steps:
- (a) inducing the ubiquitin independent degradation of the target protein which can be covalently or non-covalently linked to the N-terminus domain of antizyme by providing isolated cells with a protein consisting of the N-terminal domain portion of antizyme consisting of up to 97 amino acids or with a fusion protein consisting of the N-terminal domain portion of antizyme comprising amino acids 1-97 and of a linker recognizing the target protein with high specificity and binding the target protein with high affinity, provided that the linker is not C-terminus of antizyme;
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- (b) inducing the ubiquitin independent degradation of the target protein by covalently or non-covalently linking said protein consisting of the N-terminal domain portion of antizyme with the target protein directly or through the linker.
Dependencies are inferred from the claim text.