Targeted polypeptide degradation

Details Targeted polypeptide degradation Targeted polypeptide degradation

2008-05-13

2008-05-13

Wehbe, Anne Marie (Department: 1633)

Chemistry: molecular biology and microbiology

Measuring or testing process involving enzymes or...

Involving antigen-antibody binding, specific binding protein...

C530S350000

Reexamination Certificate

active

11003103

ABSTRACT:
This invention pertains to compositions, methods, cells and organisms useful for selectively localizing polypeptides to the proteasome for degradation. Therapeutic methods and pharmaceutical compositions for treating disorders associated with the expression and/or activity of a polypeptide by targeting these polypeptides for degradation, as well as methods for targeting therapeutic polypeptides for degradation and/or activating therapeutic polypeptides by degradation are provided. The invention provides methods for identifying compounds that mediate proteasome localization and/or polypeptide degradation. The invention also provides research tools for the study of protein function.

REFERENCES:
patent: 4522811 (1985-06-01), Eppstein et al.
patent: 4736866 (1988-04-01), Leder et al.
patent: 4870009 (1989-09-01), Evans et al.
patent: 4873191 (1989-10-01), Wagner et al.
patent: 5223409 (1993-06-01), Ladner et al.
patent: 6217864 (2001-04-01), Coffino et al.
patent: WO 90/11354 (1990-10-01), None
patent: WO 91/01140 (1991-02-01), None
patent: WO 92/0968 (1992-06-01), None
patent: WO 93/04169 (1993-03-01), None
Alberts et al., “Macromolecules: Structure, Shapes and Information,”Molecular Biology of the Cell, Chapter 3, pp. 88-91, 3d edition, Garland Publishing (1994).
Bachmair et al., “In Vivo Half-Life of a Protein Is a Function of its Amino-Terminal Residue,”Science, 234:179-186 (1986).
Baron and Bujard, “Tet Repressor-Based System for Regulated Gene Expression in Eukaryotic Cells: Principles and Advances,”Methods Enzymol.327:401-421 (2000).
Belshaw et al., “Controlling protein association and subcellular localization with a synthetic ligand that induces heterodimerization of proteins,”Proc. Natl. Acad. Sci. USA, 93:4604-4607 (1996).
Benaroudj et al., “PAN, the proteasome-activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone,”Nat. Cell Biol., 2:833-839 (2000).
Bochtler et al., “Crystal structure of heat shock locus V (HsIV) fromExcherichia coli,”Proc. Natl. Acad. Sci. U.S.A.94:6070-6074 (1997).
Bochtler et al., “The Proteasome,”Ann. Rev. Biophys. Biomol. Struct.28:295-317 (1999).
Bochtler et al., “The structures of HsIU and the ATP-dependent protease HsIU-HsIV,”Nature403:800-805 (2000).
Bradley, “Production and analysis of chimaeric mice,”Teratocarcinomas and Embryonic Stem Cells: A Practical Approach, E. J. Robertson, ed, IRL, Oxford, pp. 113-151 (1987).
Bradley, “Modifying the mammalian genome by gene targeting,”Current Opinion in Biotechnology2:823-829 (1991).
Braun et al., “The base of the proteasome regulatory particle exhibits chaperone-like activity,”Nat. Cell Biol., 1:221-226 (1999).
Carrell et al., “A Novel Procedure for the Synthesis of Libraries Containing Small Organic Molecules,”Angew. Chem. Int. Ed. Engl., 33:2059-2061 (1994).
Carrell et al., “A Solution-Phase Screening Procedure for the Isolation of Active Compounds from a Library of Molecules,”Angew. Chem. Int. Ed. Engl., 33:2061-2065 (1994).
Cho et al., “An Unnatural Biopolymer,”Science261:1303-1305 (1993).
Coffino, “Regulation of Cellular Polyamines by Antizyme,”Nat. Rev. Mol. Cell Biol., 2:188-194 (2001).
Colas et al., “Targeted modification and transportation of cellular proteins,”Proc. Natl. Acad. Sci. USA97(25):13720-13725 (2000).
Cull et al., “Screening for receptor ligands using large libraries of peptides linked to the C terminus of thelacrepressor,”Proc. Natl. Acad. Sci. USA, 89:1865-1869 (1992).
Cwirla et al., “Peptides on phage: A vast library of peptides for identifying ligands,”Proc. Natl. Acad. Sci., USA 87:6378-6382 (1990).
David et al., “Proteasomal degradation of tau protein,”J. Neurochem., 83:176-185 (2002).
Deveraux et al., “A 26 S Protease Subunit that Binds Ubiquitin Conjugates,”J. Biol. Chem., 269(10):7059-7061 (1994).
Devlin, “Random Peptide Libraries: A Source of Specific Protein Binding Molecules,”Science, 249:404-406 (1990).
DeWitt et al., “‘Diversomers’: An approach to nonpeptide, nonoligomeric chemical diversity,”Proc. Natl. Acad. Sci. USA, 90:6909-6913 (1993).
Dick et al., “Proteolytic Processing Ovalbumin and β-galactosidase by the Proteasome to Yield Antigenic Peptides,”J. Immunol., 152:3884-3894 (1994).
Erb et al., “Recursive deconvoluation of combinatorial chemical libraries,”Proc. Natl. Acad. Sci. USA, 91:11422-11426 (1994).
Farrar et al., “Activation of the Raf-1 kinase cascade by coumermycin-induced dimerization,”Nature, 383(6596):178-181 (1996).
Felici, “Selection of Antibody Ligands from a Large Library of Oligopeptides Expressed on a Multivalent Exposition Vector,”J. Mol. Biol., 222:301-310 (1991).
Fire et al., “Potent and specific genetic interference by double-stranded RNA inCaenorhabditis elegans,”Nature, 391:806-811 (1998).
Fodor, “Multiplexed biochemical assays with biological chips,”Nature, 364:555-556 (1993).
Gallop et al., “Applications of Combinatorial Technologies to Drug Discovery, . . . ,”J. Med. Chem., 37(9):1233-1251 (1994).
Glaever et al., “Functional profiling of theSaccharomyces cerevisiaegeneome,”Nature, 418:387-391 (2002).
Groll et al., “Structure of 20S proteasome from yeast at 2.4Å resolution,”Nature, 386:463-471 (1997).
Groll et al., “A gated channel into the proteasome core particle,”Nat. Struct. Biol., 7(11):1062-1067 (2000).
Groll and Huber, “Substrate access and processing by the 20S proteasome core particle,”Int. J. Biochem. Cell Biol., 35:606-616 (2003).
Güldener et al., “A new efficient gene disruption cassette for repeated use in budding yeast,”Nucleic Acids Res., 24(13)2519-2524 (1996).
Harvey et al., “Forced engagement of a RNA/protein complex by a chemical inducer of dimerization to modulate gene expression,”Proc. Natl. Acad. Sci. U.S.A., 99(4):1882-1887 (2002).
Heitman et al., “Targets for Cell Cycle Arrest by the Immunosuppressant Rapamycin in Yeast,”Science, 253:905-909 (1991).
Hershko and Ciechanover, “The Ubiquitin System,”Ann. Rev. Biochem., 67:425-479 (1998).
Ho et al., “Dimeric ligands define a role for transcription activation domains in reinitiation,”Nature, 382(6594):822-826 (1996).
Houghten, “The Use of Synthetic Peptide Combinatorial Libraries for the Identification of Bioactive Peptides,”Biotechniques, 13(3):412-421 (1992).
Jariel-Encontre et al., “Ubiquitinylation Is Not an Absolute Requirement for Degradation of c-Jun Protein by the 26 S Proteasome,”J. Biol. Chem., 270(19):11623-11627 (1995).
Jesenberger and Jentsch, “Deadly Encounter: Ubiquitin Meets Apoptosis,”Nat. Rev. Mol. Cell Biol., 3:112-121 (2002).
Kisselev et al., “The Sizes of Peptides Generated from Protein by Mammalian 26 and 20 S Proteasomes,”J. Biol. Chem., 274(6):3363-3371 (1999).
Köhler et al., “The Axial Channel of the Proteasome Core Particle Is Gated by the Rpt2 ATPase and Controls Both Substrate Entry and Product Release,”Mol. Cell, 7:1143-1152 (2001).
Kopytek et al., “Chemically induced dimerization of dihydrofolate reductase by a homobifunctional dimer of methotrexate,”Chem. Biol., 7:313-321 (2000).
Lakso et al., “Targeted oncogene activation by site-specific recombination in transgenic mice,”Proc. Nat'l Acad. Sci. U.S.A., 89:6232-6236 (1992).
Lam, “A new type of synthetic peptide library for identifying ligand-binding activity,”Nature, 354:82-84 (1991).
Lam, “Application of combinatorial library methods in cancer research and drug discovery,”Anti-Cancer Drug Des., 12:145-167 (1997).
Lam et al., “A proteasomal ATPase subunit recognize

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